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Orbital symmetry in QSAR: some Schiff's base inhibitors of carbonic anhydrase.

In a reexamination of some data on the inhibition of carbonic anhydrase (CA) isozymes I and II by some phenyl and pyridyl substituted sulfanilamide Schiff's bases we have found that activity can better be explained by considering the directions of the nodes in pi-like near frontier orbitals in the molecules. The near-frontier orbitals involved are those that are analogous to the degenerate pairs of HOMO and LUMO orbitals of benzene. This effect seems common in compounds which contain variously substituted benzene rings and is probably critical to understanding the activity of any aromatic molecule which is bound to its receptor by pi-pi charge transfer interactions.

Benzene↗

A chemiluminescense-based assay for S-nitrosoalbumin and other plasma S-nitrosothiols.

The lack of a simple assay for the quantification of S-nitrosothiols in complex biological matrices has hampered our understanding of their contribution to normal physiology and pathophysiological states. In this paper we describe an assay based upon the release of nitric oxide by reaction with a mixture consisting of Cu(I), iodine and iodide with subsequent quantification by chemiluminescense. With this method we can detect levels of S-nitrosothiols down to 5 nM in plasma. Following alkylation of free thiols with N-ethylmaleimide, and removal of nitrite with acidified sulfanilamide, we were able to measure known amounts of S-nitrosoalbumin added to plasma or whole blood, with an inter-assay variation for plasma S-nitrosothiols of approximately 4%. Further studies showed that the mean concentration of circulating S-nitrosothiols in venous plasma of healthy human volunteers was 28+/-7 nM.

Adult↗

Purification and characterization of carbonic anhydrase from bovine erythrocyte plasma membrane.

Carbonic anhydrase (CA) was purified from bovine erythrocyte plasma membrane and characterized in this study. For this purpose, the blood taken from young animals was hemolysed, the membrane fraction was separated, and this fraction was repeatedly washed. The enzyme (CA) was removed from the membrane with buffered TritonX-100 (1%); it could be purified at a factor of 22.8 by affinity chromatography. The CA obtained from erythrocyte membrane has an esterase activity as well as hydratase activity. The Vmax and Km of the enzyme for the substrate (p-nitrophenyl acetate) are 1.948x10(-3) mM/L x dak, and 3.596 mM, respectively. The purification degree of the enzyme was controlled by SDS-PAGE (3-10), which showed two distinct bands. It was determined that the enzyme had activity within the pH range of 4.5-9.5 and that the optimal pH was 7.5. The temperature at which it showed activity was 20-60 degrees C and optimal temperature was 37 degrees C. Molecular weight of CA was found to be 29844 and 61706 Dalton by gel filtration. On the other hand, sulfanilamide and acetazolamide affected the enzyme.

Animals↗

A different structural feature for carbonic anhydrases in human erythrocytes.

This study presents a different structural feature for carbonic anhydrase in human erythrocytes. Carbonic anhydrase isozymes (CA-I and CA-II) were purified from an erythrocyte pool of 20 healthy subjects. For purification, Sepharose-4B-L-tyrosine-sulfanilamide affinity column was used. Resnets from 3-10% discontinuous SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed a single band for CA-I and two distinct bands for CA-II. The molecular weights of the two bands were similar. One peak for CA-I and two peaks for CA-II were obtained in gel filtration. The enzymatic activities of the bands in question were also of different value. Native electrophoresis showed two bands for CA-I, and it showed three bands for CA-II. It can be concluded that CA-I is a polymer composed of a single promoter and CA-II has three different polymers composed of two distinct promoters, suggesting a new structural feature of human erythrocyte carbonic anhydrase isozymes.

Carbonic Anhydrases↗

Effects of melatonin on carbonic anhydrase from human erythrocytes in vitro and from rat erythrocytes in vivo.

The in vitro effects of melatonin (N-acetyl-5-methoxy-tryptamine) on human carbonic anhydrase isozymes (HCA-I and HCA-II) from human erythrocytes and in vivo effects on rat erythrocytes carbonic anhydrase (CA) were determined. Human erythrocyte carbonic anhydrase isozymes were purified by haemolysate preparation and Sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. The HCA-I enzyme, having a specific activity of 7337.5 EU/mg protein, was purified 843-fold with a yield of 60% and the HCA-II enzyme, having a specific activity of 17067EU/mg protein, was purified 1962-fold with a yield of 22.7%. For in vitro experiments, the enzyme activity was minimal at 2 x 10(-4) M melatonin concentration and increased above this concentration. Ten mgkg(-1) melatonin was administered intraperitoneally and showed a stimulatory effect on the enzyme. Time-dependent in vivo studies were conducted for melatonin in Sprague-Dawley type rats. It was found that CA activity in the rat erythrocytes was decreased by the melatonin after 1 and 3 hours to 2500 +/- 500.0 and 1875 +/- 239.4 respectively which were statistically significant (p < 0.05) differences to the control (2660 +/- 235.8). However, CA activity was restored to its normal level after 6h (2666 +/- 235.7) (p > 0.05) probably due to metabolism of the melatonin. The findings indicate that melatonin may be pharmacologically useful in some diseases.

Animals↗

Carbonic anhydrase inhibitors: aliphatic N-phosphorylated sulfamates--a novel zinc-anchoring group leading to nanomolar inhibitors.

A small library of phosphorylated sulfamates (N-(O-alkylsulfamoyl)-phosphoramidic acids) incorporating long aliphatic chains (C8-C16) has been synthesized and investigated for their interaction with two physiologically relevant carbonic anhydrase (CA) isozymes. These compounds behaved as very potent inhibitors of both isozymes, with inhibition constants in the range of 8.2-16.1nM against isozyme hCA I, and 5.3-11.9nM against isozyme hCA II. Activity was optimal for the n-octyl derivative (similarly with that of the corresponding unsubstituted sulfamates) and gradually decreased for the longer chain derivatives. Some of these compounds are much more effective CA inhibitors as compared to the clinically used derivatives acetazolamide, sulfanilamide or topiramate, which are used as standards for the enzymatic determinations. The phosphorylated sulfamate moiety represents a novel zinc-binding group for the design of effective CA inhibitors.

Binding Sites↗

Carbonic anhydrase inhibitors: Schiff's bases of aromatic and heterocyclic sulfonamides and their metal complexes.

Schiff's bases were obtained from aromatic/heterocyclic sulfonamides and amino-sulfonamide derivatives, such as sulfanilamide, homosulfanilamide, 4-aminoethyl-benzenesulfonamide and 5-amino-1,3,4-thiadiazole-2-sulfonamide. Metal complexes of some of these Schiff's bases, incorporating Zn(II), Co(lI), Ni(II) and Cu(II) ions, were also prepared and tested as inhibitors of the zinc enzyme carbonic anhydrase (CA), and more specifically the red blood cell isozymes I and II. The Schiff's bases behaved as medium potency CA I and CA II inhibitors, whereas their metal complexes showed a highly enhanced potency, with several low nanomolar CA II inhibitors detected.

Carbonic Anhydrase I↗

Synthesis and cytotoxic and analgesic activities of some 1, 5-diaryl-3-ethoxycarbonylpyrrole derivatives.

Some 1,5-diaryl-3-ethoxycarbonyl-2-methylpyrrole derivatives were obtained by reacting 1-aryl-3-ethoxycarbonylpent-1,4-diones and a suitable aniline derivative or sulfanilamide under Paal-Knorr pyrrole synthesis conditions. The cytotoxicity of the compounds was tested and all compounds, except for compound 2 h, showed a time-dependent increase in cytotoxic activity. Analgesic activities of the compounds were determined by using the tail-flick and tail-immersion methods; some of the compounds showed potent analgesic activity.

Analgesics↗

Antibacterial, antifungal and cytotoxic properties of some sulfonamide-derived chromones.

A series of antibacterial and antifungal sulfonamide (sulfanilamide, sulfaguanidine, sulfamethaxozole, 4-aminoethylbenzene-sulfonamide and 4-amino-6-trifluoromethyl-benzene-1,3-disulfonamide) derived chromones, previously reported as inhibitors of carbonic anhydrase, have been screened for in-vitro antibacterial activity against four Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Salmonella typhi and Shigella flexener) and two Gram-positive (Bacillus subtilis and Staphylococcus aureus) bacterial strains, and for in-vitro antifungal activity against Trichophyton longifusus, Candida albicans, Aspergillus flavus, Microsporum canis, Fusarium solani, Candida glaberata. All compounds (1)-(5) showed significant antibacterial activity against all four Gram-negative species and both Gram-positive species. However, three of them, (1), (4) and (5), were found to be comparatively much more active compared to (2) and (3). Of these, (5) was found to be the most active one. For antifungal activity, generally compounds (1) and (2) showed significant activity against more than three strains whereas (3)-(5) also showed significant activity against varied fungal strains. In the brine shrimp bioassay for in-vitro cytotoxic properties, only two compounds, (4) and (5) displayed potent cytotoxic activity, LD50 = 2.732 x 10(-4)M) and LD50 = 2.290 x 10(-4)M) respectively, against Artemia salina.

Animals↗

The activities of carbonic anhydrase and alkaline phosphatase in ancient human bones. Purification and characterization of outer peripheral, cytosolic, inner peripheral, and integral CA.

In the present study, bone carbonic anhydrase was isolated from ancient human bones and its characteristic features were determined. For this purpose, the skull bone of about 3000 years age was used. The purification was performed in four steps. Four different isoenzymes of CA, including outer peripheral, inner peripheral, integral, and cytosolic were purified and characterized. Affinity chromatography using Sepharose-4B-L-tyrosyn sulfanilamide as a support material was used in its purification. Two different methods were used for enzymatic activity determination: a) hydratase, and b) esterase methods. Bradford and Coomassie Brillant Blue methods were used for protein determination. Optimal pH, temperature, and molecular weight determinations were performed by conventional methods. The purification degree and the subunits, if present, were determined by SDS-PAGE. The effects of some chemicals on the enzyme were also investigated. The most cardinal finding was that the enzymatic activity has been found in antique human bone, showing some other enzymatic activity. That the alkaline phosphatase activity has been determined in the same sample supports the finding of carbonic anhydrase.

Alkaline Phosphatase↗

On the collapse of bacterial endotoxin resistance following hemorrhage.

Unanesthetized immature albino rabbits exposed to 2 hours of severe but reversible hemorrhagic shock induced with aseptic precautions by multiple cardiac bleedings exhibited no increase in susceptibility to single intravenous injections of 200 microg./kg. E. coli endotoxin administered 4 hours post retransfusion, a quantity of endotoxin that was found to be the largest dose uniformly non-lethal to normal rabbits. Paired and randomly selected rabbits treated identically except for the additional procedure of a femoral arterial cutdown and ligation (without aseptic precautions) exhibited increases in susceptibility to the same endotoxin of several hundredfold. This effect could not be attributed to the femoral cutdown and arterial ligation alone since such trauma when coupled with sham cardiac bleedings failed to increase susceptibility to 200 microg./kg. of endotoxin. These data appear valid since sham cardiac bleedings produced no detectable impairment of myocardial contractility, while 2 hours of hemorrhagic shock at 50 mm. Hg with the Lamson reservoir technique caused an increase in endotoxin susceptibility comparable to that seen when cardiac bleedings were combined with a non-sterile femoral arterial cutdown and ligation. The mechanisms increasing the susceptibility to E. coli endotoxin were investigated. It was found that (a) rabbit femoral skeletal muscle is normally contaminated with clostridia, (b) the use of aseptic femoral wounding precautions exerted some suggestive protective influence, (c) the use of aseptic wounding precautions combined with immediate topical sulfanilamide and wound closure exerted a significant protective influence, and (d) prophylactic polyvalent gas gangrene antitoxin protected in a manner not demonstrable when diphtheria antitoxin was employed as a control. These observations suggest that clostridial wound infection is one mechanism whereby a femoral arterial cutdown lowers endotoxin resistance of the rabbit following hemorrhagic shock. It is, however, not the only mechanism since the ligation of a femoral artery during hemorrhagic shock led to edema following retransfusion equivalent to a mean of approximately 30 per cent of the original circulating plasma volume. The intensification of shock caused by this transudation presumably intensified reticulo-endothelial injury, and thus further lowered the resistance of the rabbit to an intravenous injection of endotoxin 4 hours following retransfusion.

Animals↗

Factors related to the growth of psittacosis virus (strain 6BC). IV. Certain amino acids, vitamins, and other substances.

The analogues of amino acids, beta-2-thienylalanine, ethionine, and 6-methyltryptophane, inhibited the growth of psittacosis virus (6BC) in tissue culture without evidence of serious toxicity for the host cells. Of a number of vitamin analogues tested, only salicyl-beta-alanide inhibited viral multiplication in the absence of toxic effects on the host cells. 6,7-Diethylriboflavin, desoxypyridoxine, and oxythiamine reduced viral growth in concentrations that possessed some toxicity for host tissue. In tolerated amounts, 3-acetylpyridine, pyridine-3-sulfonic acid, pantoyl sulfanilamide, and desthiobiotin did not effect viral multiplication. Sodium malonate inhibited psittacosis virus growth in non-toxic amounts, whereas sodium monofluoroacetate was ineffective. Colchicine suppressed multiplication of virus only after a prolonged period of exposure and subsequent delay before producing inhibition, suggesting that the effect was secondary to its antimitotic action which suppressed multiplication of the host cells.

Alanine↗

Growth and phage production of B. megatherium. I. Growth of cells after infection with C phage. II. Rate of growth, phage yield, and RNA content of cells. III. Effect of various substances on growth rate and phage production.

I. Lysogenic B. megatherium 899a (de Jong, 1931) produces two types of phage (Gratia, 1936 c) T and C. The T phage forms cloudy plaques and gives rise to fresh lysogenic strains (Gratia, 1936 b) when added to the sensitive strain of megatherium. It may or may not cause lysis, depending on the media (Northrop, 1951). The C phage occurs very rarely) forms clear plaques, does not give rise to lysogenic strains, and causes complete lysis of the sensitive strain under all conditions tested, provided infection occurs. If C phage is added to the sensitive strain, and the mixture allowed to stand, or made into a hanging drop preparation, the infected cells stop growing and lyse completely after 60 to 80 minutes with the liberation of from 50 to 200 phage particles per cell. If, however, C phage is added to a rapidly growing culture of B. megatherium and the suspension shaken at 34 degrees , the cells continue to grow and divide for 50 to 60 minutes, after infection has occurred. They then lyse, with the liberation of from 1000 to 2500 phage particles per cell. II. The following determinations have been made on megatherium sensitive cells growing in 5 per cent peptone at different stages of growth. (1) Growth rate of infected and uninfected cells; (2) RNA, DNA, and protein content; (3) volume of the cell; (4) phage yield per cell by plaque count; (5) phage yield per cell by cell and plaque count; (6) lysis time. The growth rate decreases as the cell concentration increases. The lysis time and the protein N per cell are nearly independent of the growth rate; all the other values increase as the growth rate increases. The ratio See PDF for Equation is nearly constant. RNA and DNA per cell increase less rapidly than the volume, so that NA per unit volume is not constant, but decreases as the size of the cell increases. The phage yield measured under conditions in which the infected cells do not grow (by plaque count) is very nearly proportional to the size of the cell. The phage yield per cell, under conditions in which the infected cells do grow, increases more rapidly than the size of the cells. The phage yield per cell under these conditions may be calculated by the equation See PDF for Equation The determining factor for the variation in phage yield is the growth rate of the cells. This, in turn, is determined by the composition of the medium. III. The growth and phage production of megatherium 899a have been determined in the presence of the following substances: aureomycin, bacitracin, chloromycetin, gramicidin, Merck AB631, Merck AB191, Merck AB624, penicillin, streptomycin, terramycin, tyrothricin, usnic acid, acetone, chloroform, ethyl alcohol, formaldehyde, gentian violet, glycerin, maleic hydrazide, methyl alcohol, phenyl mercuric acetate, sodium fluoride, sulfanilamide, toluene, and urethane. In every case, the lowest concentration of the substance which completely inhibits growth, is also the lowest concentration which completely inhibits phage production. One antibiotic, Merck AB81, causes increased phage production in concentrations which partially inhibit growth, and low phage production in concentrations which completely inhibit growth (as determined by turbidity). Short exposure to ultraviolet light also decreases the growth rate, with increase in phage production. Longer exposure, which completely inhibits growth (as determined by turbidity) results in lysis and phage liberation.

Bacillus↗

Pantothenic acid, coenzyme A, and human chronic ulcerative and granulomatous colitis.

To investigate further an apparent relationship between chronic ulcerative and granulomatous colitis and pantothenic acid deficiency, colonic tissues obtained at the time of colectomy in 29 patients with these disorders were assayed for pantothenic acid and for coenzyme A (CoA) activity. For comparison, normal colonic tissues free of pathological lesions were obtained from 31 patients having colectomy for carcinoma or diverticulitis. Plasma, red blood cells, and colonic mucosa were assayed microbiologically for free and total pantothenic acid. The activity of CoA in colonic mucosa was determined by assaying the acetylation of sulfanilamide. Concentrations of free, bound, and total pantothenic acid in blood and in colonic mucosa did not differ between the two groups of patients. Bound pantothenic acid increased linearly with total pantothenic acid. Colonic mucosa concentrated free pantothenic acid to about 50 times the level of blood, and pantothenic acid in red cells was similar to the concentration in plasma. Compared to normal gut mucosa, CoA activity was markedly low in mucosa from patients with chronic ulcerative or granulomatous disease despite the presence of normal amounts of free and bound pantothenic acid. A block in the conversion of bound pantothenic acid to CoA in diseased mucosa is suggested.

Adult↗

N-acetylation and N-formylation of carcinogenic arylamines and related compounds in dogs.

When sulfanilamide, p-aminobenzoic acid, 4-amino-biphenyl, 2-aminofluorene or 1-aminopyrene was given orally to dogs, the corresponding N-acetyl and N-formyl derivates were isolated from urine or feces. These metabolites were identified unequivocally by comparison with an authentic sample by UV and mass spectrometry and their behaviour in TLC and HPLC. Dog intestinal flora and several bacterial strains exhibited both N-acetylating and N-formylating activities, in varying degrees, toward all of the arylamines tested. The metabolites formed by the intestinal bacteria were also isolated and identified unequivocally. The results suggest that the intestinal microflora plays an important role in the formation of N-acyl derivatives from arylamines in dogs.

Acetylation↗

Recombination as a requirement for segregation of a partially diploid mutant of Pneumococcus.

Conditions are described in which the pneumococcal mutant strain sulr-c, resistant to the drug sulfanilamide, gives rise to sensitive segregants resistant to nitrobenzoic acid at a frequency constant with time. This segregant frequency is markedly enhanced upon exposure of the cells to doses of ultraviolet light or mitomycin C that permit survival of 50% to 90% of the cells. Treatment with acridine orange diminishes the segregant frequency. From the known influences of these three agents on genetic recombination, we propose that a recombination event is necessary in the generation of segregants.--During a period of incubation following treatment with ultraviolet light or mitomycin C, cell division resumes and the original segregant frequency is restored. Thus potential segregants are either unable to replicate in the absence of selection, or they are under-represented among the cells dividing soon after treatment.--If the sulr-c mutation is introduced into a mutant pneumococcal strain lacking an ATP-dependent exonuclease activity and deficient in recombination with transforming DNA, segregant frequencies are unaffected. This fact may indicate limits upon the type of recombination event responsible for segregation.

Acridines↗

Evaluation of reagent strips for the rapid diagnosis of nitrite poisoning.

Two commercial urine test strips based on the Griess nitrite-specific diazonium salt reaction, having sulfanilamide and para-arsanilic acid as substrates, respectively, were studied as qualitative tests in the rapid diagnosis of nitrite/nitrate poisoning. Their usefulness was compared to other rapid tests, such as the sulfanilic acid-1 naphthylamin and diphenylamine blue tests. The practical sensitivity limit to nitrites in plasma and in water of both the reagent strips and SA-1NA test was 0.50 micrograms NO2/mL, while the diphenylamine test, which is not nitrite specific, showed a positive reaction to nitrites in plasma and in water above 50 micrograms NO2/mL and 5 micrograms NO2/mL, respectively. The in vitro assays were evaluated in vivo by the sublethal intoxication of a sheep with nitrite, demonstrating that commercial urine test strips may be useful for the rapid diagnosis of nitrite/nitrate poisoning.

Evaluation Studies as Topic↗

Identification and expression of cotton (Gossypium hirsutum L.) plastidial carbonic anhydrase.

Four carbonic anhydrase (CA) cDNA clones were isolated from a 48 h dark-grown cotton (Gossypium hirsutum L.) seedling cDNA library. Nucleotide sequence analysis revealed two different CA isoforms designated GhCA1 and GhCA2. The encoded polypeptides possess N-terminal serine/threonine-rich regions indicative of plastid transit peptides, and approximately 80% sequence identity to other plant plastidial beta-CAs. The GhCA1 cDNA encodes a nearly complete preprotein of 323 amino acids with a molecular mass of 34.9 kDa and a predicted mature protein of 224 amino acids with a molecular mass of 24.3 kDa. Eleven nucleotide differences within ORFs of GhCA1 and GhCA2 result in 5 conservative amino acid substitutions. The 3' GhCA2 untranslated region contains five additional substitutions and one single nucleotide addition. GhCA1 clones, nearly full-length or with 70% of the transit peptide deleted, were expressed as LacZ alpha fusion proteins in E. coli. Lysates of these strains contained 9-fold higher levels of CA activity as compared to untransformed controls and this activity was inhibited by CA-specific inhibitors. Sulfanilamide, acetazolamide, ethoxyzolamide, each at 10 mM, inhibited recombinant CA activity approximately 50%, 65%, and 75%, respectively. In plant tissue homogenates these inhibitors reduced CA activity by 50%, 70%, and 95%, respectively. Although CA activity was bighest in extracts of mature cotton leaves, probing total RNA with GhCA1 revealed CA transcript levels to be highest in the cotyledons of dark-grown cotton seedlings. Collectively, our data indicate the presence of a plastid-localized CA in cotyledons of germinated seeds, suggesting a role for CA in postgerminative growth.

Amino Acid Sequence↗