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PubMed1984

Acyltransferase-catalyzed cleavage of arachidonic acid from phospholipids and transfer to lysophosphatides in macrophages derived from bone marrow. Comparison of different donor- and acceptor substrate combinations.

In a previous paper it was shown that in prelabeled murine thymocytes a direct CoA-mediated transfer of arachidonic acid from phosphatidylcholine to lysophosphatidylethanolamine occurs which does not involve the intermediate formation of free fatty acid. The transfer is ATP-independent and is catalyzed by the acyl-CoA: lysophosphatide acyltransferase operating in reverse. In prelabeled thymocytes phosphatidylcholine was the only arachidonoyl donor and lysophosphatidylethanolamine the only lysoacceptor. In murine bone-marrow-derived macrophages a series of CoA-mediated transfer reactions were detected leading to a redistribution of arachidonic acid between phospholipids. Using exogenous substrates a bidirectional transfer from 1-acyl-2-arachidonoylglycerophosphocholine to lysophosphatidylethanolamine occurs. An unidirectional transfer from 1-acyl-2-arachidonoylglycerophosphoinositol to lysophosphatidylcholine and from 1-acyl-2-arachidonoylglycerophosphoinositol to lysophosphatidylethanolamine was observed. Plasmalogenic lysoacceptors generally have a weaker acceptor capacity than the correspondent acyllysophospholipid. In macrophages the CoA-mediated transfer of arachidonoyl moieties is independent of ATP and Mg2+ and is totally inhibited by sodium cholate, indicating that it is catalyzed by the acyl-CoA: lysophosphatide acyltransferase.

Acyltransferases↗

PubMed1987

Subunit composition of the H+-ATPase complex from anaerobic bacterium Lactobacillus casei.

The H+-ATPase complex has been isolated from the membranes of the anaerobic bacterium Lactobacillus casei by two independent methods. 1. The crossed-immunoelectrophoresis of the 14C-labelled ATPase complex against antibodies to a highly purified soluble ATPase has been used. The subunit composition of the complex has been established by autoradiography. The soluble part of L. casei ATPase, in contrast to coupling factor F1-ATPases of aerobic bacteria, chloroplasts and mitochondria which include two kinds of large subunit (alpha and beta), consists of one kind of large subunit with a molecular mass of 43 kDa. Moreover, a minor polypeptide of 25 kDa has been found in the soluble ATPase. Factor F0 of L. casei ATPase complex consists of a 16-kDa subunit and two subunits with molecular masses less than 14 kDa. 2. A dicyclohexylcarbodiimide-sensitive ATPase complex has been isolated from L. casei membranes by treating them with a mixture of octyl glucoside and sodium cholate. The complex, purified by centrifugation on a sucrose density gradient, contains the main subunits with molecular masses of 43 kDa, 25 kDa and 16 kDa and a dicyclohexylcarbodiimide-binding subunit with a molecular mass less than 14 kDa.

Adenosine Triphosphatases↗

PubMed1990

Purification and characterization of heme oxygenase from chick liver. Comparison of the avian and mammalian enzymes.

A major inducible form of heme oxygenase (EC 1.14.99.3) was purified from liver microsomes of chicks pretreated with cadmium chloride. The purification involved solubilization of microsomes with Emulgen 913 and sodium cholate, followed by DEAE-Sephacel, carboxymethyl-cellulose (CM-52) and hydroxyapatite chromatography, and FPLC through Superose 6 and 12 columns operating in series. The final product gave a single band on silver-stained SDS/polyacrylamide gels (Mr = 33,000). Optimal conditions for measurement of activity of solubilized heme oxygenase were studied. In a reconstituted system containing purified heme oxygenase, NADPH-cytochrome reductase, biliverdin reductase and NADPH, the Km for free heme was 3.8 +/- 0.5 microM; for heme in the presence of bovine serum albumin (5 mol heme/3 mol albumin) the Km was 5.0 +/- 0.8 microM; and the Km for NADPH was 6.1 +/- 0.4 microM (all values mean +/- SD, n = 3). Oxygen concentration as low as 15 microM, with saturating concentrations of heme and NADPH, did not affect the reaction rate, indicating that the supply of oxygen is not involved in the physiological regulation of activity of the enzyme. The pH optimum of the reaction was 7.4; at 37 degrees C, the apparent Vmax was 580 +/- 44 nmol biliverdin.(mg protein)-1.min-1 and the molecular activity was 19.2 min-1. Biliverdin IXa was the sole biliverdin isomer formed. In the presence of purified biliverdin reductase, biliverdin was converted quantitatively to bilirubin. Addition of catalase to the reconstituted system decreased the breakdown of heme to non-biliverdin products and led to nearly stoichiometric conversion of heme to biliverdin. Activity of the enzyme in the reconstituted system was inhibited by metalloporphyrins in the following order of decreasing potency: tin mesoporphyrin greater than tin protoporphyrin greater than zinc protoporphyrin greater than manganese protoporphyrin greater than cobalt protoporphyrin. Protoporphyrin (3.3 or 6.6 microM) (and several other porphyrins) and metallic ions (100 microM) alone had little if any inhibitory effect, except for Hg2+ which inhibited by 67% at 10 microM and totally at 15 microM. Following partial cleavage, fragments of the purified enzyme were sequenced. Comparison of sequences to those derived from cDNA sequences for the major inducible rat and human heme oxygenase showed 69% and 76% similarities, respectively. The histidine residue at position 132 of rat heme oxygenase-1 and the residues (Lys128-Arg136) flanking His132 were conserved in all three enzymes, as well as in the corresponding portion of a fourth less highly similar rat enzyme, heme oxygenase-2.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗

PubMed1996

Changes in plasma phospholipids in the presence and absence of erythrocytes 31P-NMR time-course studies.

Whole human blood and plasma were incubated at 37 degrees C and 31P-NMR spectra were acquired from aliquots of plasma dissolved in sodium cholate. The narrow resonances of phospholipids were well resolved, allowing identification and accurate quantification of the various phospholipid classes. During the course of plasma incubation, the rate of increase in 2-lysphosphatidylcholine (2-LysoPtdCho) corresponded closely to the rate of decrease in phosphatidylcholine. However, little or no change was observed in the sphingomyelin concentrations. The rate of cholesteryl ester formation in plasma was also determined using HPLC and was observed to be similar to the rate of 2-LysoPtdCho increase in plasma; this is consistent with the rate of acyl transfer from phosphatidylcholine to free cholesterol catalysed by lecithin:cholesterol acyltransferase. However, during the course of whole blood incubation, the rate of 2-LysoPtdCho increase in plasma was significantly lower than the rate of 2-LysoPtdCho production during incubation of plasma alone (31 +/- 4 micromol x 1(-1) x h(-1) and 80 +/- 8 micromol x 1(-1) x h(-1), respectively). The difference between the rates can be attributed to the action of enzymes present in blood cells including those in the erythrocytes that catalyse acylation or hydrolysis of 2-LysoPtdCho.

Chromatography, High Pressure Liquid↗

PubMed1996

Structural properties of the putative fusion peptide of hepatitis B virus upon interaction with phospholipids. Circular dichroism and Fourier-transform infrared spectroscopy studies.

A peptide corresponding to the N-terminal sequence of the S protein from hepatitis B virus (Met-Glu-Asn-Ile-Thr-Ser-Gly-Phe-Leu-Gly-Pro-Leu-Leu-Val-Leu-Gln) has been previously shown to interact with phospholipids and promote vesicle aggregation, phospholipid mixing, and liposome leakage, as well as erythrocyte lysis [Rodríguez-Crespo, I., Núñez, E., Gómez-Gutiérrez, J., Yélamos, B., Albar, J. P., Peterson, D. L. & Gavilanes, F. (1995) J. Gen. Virol. 76, 301-308]. The conformation of this putative fusion peptide has been studied, both at low and high peptide concentrations, by means of circular dichroism and Fourier-transform infrared spectroscopy, respectively. When the peptide is dissolved in trifluoroethanol, a significant population of alpha-helical structure is found in spite of the proline residue at position 11. In contrast, this hydrophobic oligopeptide has a high tendency to form large beta-sheet aggregates in aqueous buffers. Most of these aggregates can be eliminated by centrifugation. The peptide remaining in the supernatant adopts a non-ordered conformation. The aggregates can be dissociated by the anionic detergent sodium cholate, but the peptide still maintains an extended conformation. In the presence of acidic phospholipid vesicles, the putative fusion peptide adopts a highly stable beta-sheet conformation. Thus, unlike the fusion peptides of other viruses, an extended conformation seems to be the preferred structure when interacting with phospholipids. Such a conformation should be responsible for its membrane destabilization properties.

Amino Acid Sequence↗

PubMed1996

Biochemical evidence for membrane-bound endoderm-specific alkaline phosphatase in larvae of the ascidian, Halocynthia roretzi.

An endoderm-specific alkaline phosphatase with a molecular mass of 86 kDa has been found in tadpole larvae of the ascidian, Halocynthia roretzi. The histochemical staining of sections of the larvae revealed that the enzyme is a membrane-associated protein. Two distinct bands were detected by zymographic technique on SDS/PAGE of the membrane preparation of the larvae. The two enzymes can be solubilized from the membrane preparation by sodium cholate and separated from each other by Cibacron blue-3GA affinity chromatography. The 86-kDa enzyme is likely to be the endoderm-specific one because the susceptibilities to alkaline phosphatase inhibitors coincide between the 86-kDa enzyme and that found in the endoderm of larvae by histochemical staining. The endoderm-specific alkaline phosphatase was purified and its N-terminal amino acid sequence was found to show little similarity to those of other proteins.

Alkaline Phosphatase↗

PubMed1997

Changes in cellular and plasma membrane phospholipid composition after lipopolysaccharide stimulation of human neutrophils, studied by 31P NMR.

Lipopolysaccharide (endotoxin, LPS) exerts potent proinflammatory effects on neutrophils which may involve membrane phospholipid metabolism. The cellular and plasma membrane phospholipid composition of resting neutrophils and those stimulated with 50 microg ml(-1) LPS were studied by 31P NMR and chemical analysis. A rapid new method for plasma membrane purification was employed, involving the direct lysis of cytoplasts. Chemical analyses showed that, although total cellular phospholipid content did not change with LPS stimulation, there was twice the amount of phospholipid present in plasma membranes isolated from stimulated cells, resulting in a lowered cholesterol/phospholipid ratio. Since internal membranes have lower cholesterol content this result is consistent with an origin from insertion of these membranes (most probably from the endoplasmic reticulum) into the plasma membrane, thereby increasing its fluidity. The individual phospholipid classes of both cells and membranes were quantified by 31P-NMR spectroscopy after dissolution in sodium cholate without prior extraction of lipids, allowing partial resolution of the major phospholipid classes and ether-linked phospholipids. Ether-linked lipids were distinguished from diacyl phospholipids by hydrolysis of lipid extracts with HCl and phospholipase A1, There was a significant increase in phosphatidylserine in both cells and plasma membranes after stimulation, with a decrease in the phosphatidylethanolamine (diacyl and plasmalogen) content in the cells. Plasma membranes from stimulated cells exhibited a significant decrease in a phospholipid tentatively identified as 2-arachidonoyl-1-alkyl-sn-glycero-3-phosphocholine, a precursor of the lipid inflammatory mediator, platelet-activating factor. This report is the first to elaborate the changes in phospholipid composition in human neutrophils as a whole, and in plasma membranes separated from them, before and after stimulation by the physiological activator, LPS.

Cell Compartmentation↗

PubMed1987

Alkylation of free sulfhydryls fortifies electroplax subsynaptic structures.

The cysteine-rich 43,000-dalton peripheral membrane protein, nu 1, is localized at the cytoplasmic face of electroplax and muscle cholinergic synapses, where it is thought to play an important role in the endplate supramolecular structure. The peripheral membrane protein properties of nu 1 are inferred by its removal from nicotinic cholinergic membranes by the action of mild alkali or lithium diiodosalicylate. An interesting property of nu 1 is its high concentration of free sulfhydryl groups, whose exact role in synaptic structure is still largely unknown. Alkylation of free sulfhydryls with N-ethylmaleimide (3 mM) has a profound effect on the association of nu 1 with synaptic membranes, rendering nu 1 unextractable by pH 11 treatment or by lithium diiodosalicylate and, concomitantly, decreasing nu 1's electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gels. Iodoacetamide and iodoacetate have similar effects, but at concentrations 10- to 100-fold higher than required for N-ethylmaleimide. Furthermore, sulfhydryl modification also stabilizes the association of nicotinic receptor subunits with the detergent-insoluble cytoskeleton. N-Ethylmaleimide treatment increases the fraction of insoluble receptor molecules on extraction with Triton X-100, sodium cholate, or octylglucoside. These results suggest an important role of sulfhydryl groups in the structural stability of the postsynaptic cholinergic membrane.

Alkylation↗

PubMed1987

Highly sensitive immunoassay for the alpha subunit of the GTP-binding protein go and its regional distribution in bovine brain.

Antisera were raised in rabbits against the alpha subunit of a GTP-binding protein, Go. Because the antisera cross-reacted weakly with the alpha subunit of inhibitory GTP-binding protein of adenylate cyclase (Gi), they were purified with a Go alpha-coupled Sepharose column. Purified antibodies reacted only with Go alpha and did not cross-react with the Gi alpha subunit or beta gamma subunits in an immunoblot assay. Using these purified antibodies, a highly sensitive enzyme immunoassay method for the quantification of bovine brain Go alpha was developed. The assay system consisted of polystyrene balls with immobilized antibody F(ab')2 fragments and the same antibody Fab' fragments labeled with beta-D-galactosidase from Escherichia coli. The minimal detection limit of the assay was 0.1 fmol, or 4 pg. The assay was specific for Go alpha, and it did not cross-react with Gi alpha or beta gamma. Samples from various regions of bovine brain were solubilized with 2% sodium cholate and 1 M NaCl, and the concentrations of Go alpha were determined. Go alpha was detected in all the regions, and the highest concentration was observed in the cerebral cortex. The immunohistochemical study showed that the neuropil was rich in Go alpha.

Animals↗

PubMed1988

Solubilization of rat brain phencyclidine receptors in an active binding form that is sensitive to N-methyl-D-aspartate receptor ligands.

Phencyclidine (PCP) receptors were successfully solubilized from rat forebrain membranes with 1% sodium cholate. Approximately 58% of the initial protein and 20-30% of the high-affinity PCP binding sites were solubilized. The high affinity toward PCP-like drugs, the stereo-selectivity of the sites, and the sensitivity to N-methyl-D-aspartate (NMDA) receptor ligands were preserved. Binding of the potent PCP receptor ligand N-[3H][1-(2-thienyl)cyclohexyl] piperidine ([3H]TCP) to the soluble receptors was saturable (KD = 35 nM), and PCP-like drugs inhibited [3H]TCP binding in a rank order of potency close to that observed for the membrane-bound receptors; the most potent inhibitors were TCP (Ki = 31 nM) and the anticonvulsant MK-801 (Ki = 50 nM). The NMDA receptor antagonist 2-amino-5-phosphonovaleric acid inhibited binding of [3H]TCP to the soluble receptors; glutamate or NMDA diminished this inhibition in a dose-dependent manner. Taken together, the results indicate that the soluble PCP receptor preparation contains the glutamate recognition sites and may represent a single receptor complex for PCP and NMDA, as suggested by electrophysiological data. The successful solubilization of the PCP receptors in an active binding form should now facilitate their purification.

2-Amino-5-phosphonovalerate↗

PubMed1989

Solubilization and characterization of sigma-receptors from guinea pig brain membranes.

The sigma-receptor, a distinct binding site in brain tissue that may mediate some of the psychotomimetic properties of benzomorphan opiates and phencyclidine, has been solubilized using the ionic detergent sodium cholate. Binding assays were performed with the solubilized receptor using vacuum filtration over polyethyleneimine-treated glass fiber filters. The pharmacological specificity of the solubilized binding site for sigma-receptor ligands is nearly identical to the membrane-bound form of the receptor, with the order of potencies for displacement of the selective sigma-ligand [3H]di-o-tolylguanidine ([3H]DTG) closely correlated. The stereoselectivity for (+)-benzomorphan opiate enantiomers was retained by the solubilized receptor. The soluble receptor retained high affinity for binding of [3H]DTG (KD = 28 +/- 0.5 nM) and (+)-[3H]3-(3-hydroxyphenyl)-N-(1-propyl)piperidine [(+)-[3H]3-PPP] (KD = 36 +/- 2 nM). Photoaffinity labeling of the solubilized receptor by [3H]p-azido-DTG, a sigma-selective photoaffinity label, resulted in labeling of a 29-kilodalton polypeptide identical in size to that labeled in intact membranes. Estimation of the Stokes radius of the [3H]DTG binding site was obtained by Sepharose CL-6B chromatography in the presence of 20 mM cholate and calculated to be 8.7 nm. This value was identical to the molecular size found for the binding sites of the sigma-selective ligands (+)-[3H]3-PPP and (+)-[3H]SKF-10,047, supporting the hypothesis that all three ligands bind to the same macromolecular complex.

Affinity Labels↗

PubMed2006

Evaluation of inactivation methods for severe acute respiratory syndrome coronavirus in noncellular blood products.

BACKGROUND: Severe acute respiratory syndrome coronavirus (SARS-CoV) has been detected in the blood of infected individuals, which may have the potential to contaminate donated blood and plasma-derived products in the event of a future outbreak. Effective methods for inactivating the SARS-CoV in protein solutions are described in this report. STUDY DESIGN AND METHODS: Heat, ultraviolet (UV) irradiation, octanoic acid, and solvent/detergent (S/D) methods were tested individually for their ability to inactivate SARS-CoV in protein solutions appropriately mimicking blood-derived products. Treated samples were tested for inactivation in a tissue culture growth assay. RESULTS: Viral inactivation by heat treatment at 60 degrees C required 15 to 30 minutes to inactivate the SARS-CoV. UVC efficiently inactivated SARS-CoV in 40 minutes, whereas UVA required the addition of psoralen to enhance inactivation of the virus. The presence of bovine serum albumin limited the ability of UVC and UVA to inactivate SARS-CoV and octanoic acid treatment does not reduce the infectivity of SARS-CoV-spiked protein solutions. S/D treatment required 2, 4, and up to 24 hours for Triton X-100, Tween 80, and sodium cholate inactivation, respectively. CONCLUSION: Heat, UVC irradiation, and S/D treatments effectively inactivate SARS-CoV, whereas octanoic acid treatment is insufficient for inactivation of the virus.

Animals↗

PubMedDate not supplied

Effects of bile salt-stimulated lipase-treated triglycerides and free fatty acids on extracellular stages of Eimeria tenella.

Normal human milk (NHM) has antiprotozoal activity unrelated to immunological components; this activity extends to sporozoites of Eimeria tenella. This activity may be due to free fatty acids (FFA) enzymatically hydrolyzed from triacyl glycerols by a bile salt-stimulated lipase (BSSL) found in NHM. Sporozoites were therefore incubated in the presence of several saturated and unsaturated FFA. Anticoccidial activity was observed for many unsaturated fatty acids and for some saturated fatty acids. In addition, sporozoites were added to solutions of triglycerides (trilinolein, triolein and trilinolenin) preincubated with BSSL and sodium cholate, which resulted in killing of the parasites. Triglycerides alone showed no anticoccidial activity. These results were duplicated with first generation merozoites. Intracellular stages of E. tenella were affected by FFA only at concentrations that inhibited host cells.

Animals↗

PubMed1988

Solubilization of vitamin K1 by bile salts and phosphatidylcholine-bile salts mixed micelles.

The solubilization of vitamin K1 by bile salts (sodium deoxycholate, sodium cholate and their corresponding glycine conjugates) and phosphatidylcholine (egg)-bile salt mixed micelles has been investigated. The solubilization curves were not always linear with increasing bile salts, but the vitamin was appreciably solubilized in the region below their CMCs. In the bile salt solutions (20 mM, phosphate buffered saline, pH 7.5, ions strength 0.2), the solubilized vitamin ranged from 0.3 to 0.9 mM. With increasing phosphatidylcholine, the amount of vitamin solubilized was dramatically increased; at the molar ratio of 1:1 (both 20 mM), the amount of vitamin solubilized was about 25-30 times more than by the corresponding bile salts alone. There is a possibility that exogenous phospholipid given orally as liposomal forms assists the solubilization of vitamin K1, in the intestine. This characteristic is suggested as being responsible, in part, for the enhanced recovery of blood coagulation after oral administration of liposomal vitamin K1 to warfarin-treated rabbits.

Bile Acids and Salts↗

PubMed1982

Solubilized adenosine receptors in the brain: regulation of guanine nucleotides.

Adenosine receptors associated with a reduction of adenylate cyclase and labeled by tritium-labeled cyclohexyladenosine can be solubilized from brain membranes with sodium cholate. Regulation of receptor binding by guanine nucleotides is retained in the soluble state. Influences of cations observed in membrane preparations of adenosine receptors are no longer detected with the solubilized receptors. The apparent retention of a complex of receptors and guanosine triphosphate binding but not cation binding protein in the soluble state may permit a molecular analysis of receptor regulation.

Adenosine↗

PubMed1983

In vitro antibacterial properties of AT-2266, a new pyridonecarboxylic acid.

AT-2266, 1-ethyl-6-fluoro-1,4-dihydro-4-oxo-7-(1-piperazinyl)-1,8-naphthyridine-3 -carboxylic acid, is a new pyridonecarboxylic acid derivative with broad and potent antibacterial activity. It inhibited some gram-positive bacteria, such as staphylococci and Bacillus subtilis, and most gram-negative bacteria, including Serratia marcescens, Pseudomonas aeruginosa, Haemophilus influenzae, and Campylobacter jejuni, at concentrations of 0.1 to 0.78 microgram/ml, and most gram-positive bacteria, glucose-nonfermenters, and Mycoplasma pneumoniae at concentrations of 1.56 to 12.5 micrograms/ml. Most of the clinical isolates tested were as susceptible to AT-2266 as were laboratory strains. The antibacterial potency of AT-2266 was higher than those of pipemidic acid and nalidixic acid and similar to that of norfloxacin. AT-2266 was not cross-resistant with antibiotics and inhibited most highly nalidixic acid-resistant bacteria at concentrations of 1.56 to 3.13 micrograms/ml. Its activity was barely affected by the addition of horse serum or sodium cholate but weakened by lowering the medium pH or increasing the inoculum size. AT-2266 was bactericidal at concentrations near its minimal inhibitory concentrations. Frequencies of mutants resistant to 10 micrograms of AT-2266 per ml were lower than 4.0 x 10(-9).

Anti-Bacterial Agents↗

PubMed1985

In vitro activity of CI-934, a quinolone carboxylic acid active against gram-positive and -negative bacteria.

CI-934 is a totally synthetic difluorinated quinolinecarboxylic acid with an ethyl-amino-methyl pyrrolidine side chain, which has broad-spectrum antibacterial activity, including particular potency directed against streptococci and staphylococci. The CI-934 MIC (micrograms per milliliter) for 90% of the strains tested was 0.4 (range, 0.2 to 0.8) for a group of streptococci (pneumococci, viridans streptococci, Streptococcus faecalis, and Lancefield groups A, B, and C), 0.2 (0.05 to 0.2) for staphylococci (including methicillin-resistant Staphylococcus aureus), 0.025 (less than or equal to 0.003 to 0.025) for Haemophilus influenzae and Neisseria gonorrhoeae, 1.6 (0.1 to 25) for Enterobacteriaceae, 25 (3.1 to 25) for Pseudomonas aeruginosa, and 1.6 (0.05 to 3.1) for non-Bacteroides anaerobe species. CI-934 was equally active in vitro against multi-drug-resistant and -sensitive isolates, and cross-resistance was not apparent. Potency increased with alkalinity and was somewhat lower in urine. CI-934 was bactericidal. Inhibitory activity was generally unaffected by anaerobiosis, light, changes in inoculum size or cation concentration, or addition of human serum or sodium cholate.

Anaerobiosis↗

PubMed1975

Pipemidic acid, a new antibacterial agent active against Pseudomonas aeruginosa: in vitro properties.

Pipemidic acid, 8-ethyl-5,8-dihydro-5-oxo-2-(1-piperazinyl)-pyrido [2,3-d]pyrimidine-6-carboxylic acid, is a new derivative of piromidic acid. It is active against gram-negative bacteria including Pseudomonas aeruginosa as well as some gram-positive bacteria. Its potency is generally greater than that of piromidic acid and nalidixic acid. Cross-resistance is not observed between pipemidic acid and various antibiotics, and most of bacteria resistant to piromidic acid and nalidixic acid are moderately susceptible to pipemidic acid. The activity of pipemidic acid is scarcely affected by the addition of serum, sodium cholate, or change of medium pH, but is subject to the influence of inoculum size. Its action is bactericidal above minimal inhibitory concentrations.

Bacteria↗