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At least 307 records · Page 17Linked to original sources
PubMed1979

An approach to the routine estimation of circulating carcinoembryonic antigen immune complexes in patients with carcinomata of the gastrointestinal tract.

The carcinoembryonic antigen (CEA) distribution obtained after fractionation of thirty sera of patients with gastrointestinal tumours by gel filtration in Sephadex G200 was compared with that resulting from extraction of the sera with perchloric acid. In all cases gel filtration yielded a fraction of free CEA and in twenty-three cases an additional fraction of CEA immune complexes. The amounts of free CEA corresponded fairly well to the fractions of CEA which could be extracted by perchloric acid. The CEA content of the fraction containing CEA immune complexes was comparable to the CEA content of the perchloric acid precipitates. The presence of CEA immune complexes in the perchloric acid precipitates could be demonstrated by gel filtration under dissociating andnon-dissociating conditions and after pre-incubation with 125I-CEA by radioimmuno-double-diffusion using monospecific rabbit antisera against human IgM and IgG.

Adenocarcinoma↗
PubMedDate not supplied

Recombinant perchloric acid-soluble protein suppresses the immunoglobulin production of human-human hybridoma HB4C5 cells.

Because perchloric acid-soluble protein (PSP) has been conserved evolutionally in various species from Escherichia coli to humans, it may reflect an involvement in basic cellular regulation. However, the precise function of PSP is currently unknown. In this study, we examined the direct effect of PSP on the production of immunoglobulin (Ig) using human B, HB4C5, NAT-30, and U266 cells because it has been reported that subcutaneous administration of PSP affects rodent immune systems. Suppression of Ig productivity and decrement of the cell viability was recognized only in HB4C5 cells by the addition of PSP into the medium. On the other hand, PSP had no effect on Ig productivity and cell viability in NAT-30 and U266 cells. In addition, PSP was clearly incorporated by HB4C5 but not by the other cells. These results suggest that the Ig production suppressed by PSP, which has been previously reported to inhibit protein synthesis, contributed to the incorporation of PSP into the HB4C5 cells.

Animals↗
PubMed1995

Superiority of acid extractable glycogen for detection of metabolic changes during myocardial ischaemia.

Various methods for extraction and isolation of myocardial glycogen show different yields and identify different glycogen subsets. The aim of the present study was to identify a glycogen fraction exposed to changes during myocardial ischaemia. Endomyocardial biopsies from 10 pigs were sampled before cardioplegia, after cardioplegic arrest, and after reperfusion. Glycogen yields were compared following five extraction procedures: (1) hot alkaline tissue digestion, (2) homogenization in perchloric acid and subsequent determination in homogenate, (3) homogenization in perchloric acid and subsequent determination in supernatant, (4) homogenization in perchloric acid and subsequent determination in the precipitate redissolved in hot alkaline and (5) homogenization in homogenisation buffer with lysating capacity. Glycogen was isolated on filter-paper and determined enzymatically. Hot alkaline tissue digestion yielded the highest glycogen amounts (63.5 +/- 18.3 nmol/mg wet weight). Glycogen yields in perchloric homogenate and supernatant were 51%, perchloric precipitate 47%, and buffer 30% of these obtained with hot alkaline. Glycogen yields in hot alkaline were comparable to the sum of those obtained in perchloric supernatant ("acid extractable glycogen") and redissolved precipitate ("heavily extracted glycogen") confirming that glycogen yields obtained with hot alkaline digestion represent "total glycogen". Acid extractable glycogen showed superior analytical characteristics compared with the other methods. Acid extractable glycogen demonstrated a consistent decrease during ischaemia whereas total glycogen and glycogen extracted in homogenization buffer tended to decrease. Glycogen in perchloric precipitate remained unchanged during ischaemia. These findings support a revival of the concept that tissue contains two forms of glycogen. Decreases in myocardial glycogen content during myocardial ischaemia are best observed with acid extractable glycogen.

Animals↗
PubMed2005

Perchloric acid-soluble protein regulates cell proliferation and differentiation in the spinal cord of chick embryos.

The role of perchloric acid-soluble protein (PSP) was investigated in chick embryos. Fluorescently labeled anti-chick liver (CL)-PSP IgG was injected into the yolk sac in ovo at embryonic day 3, and became localized in neuroepithelial cells. Within 12 h, morphological changes were observed in 37.5% of anti-CL-PSP IgG-injected embryos, and the neuroepithelial cells formed a wavy line. No significant changes were observed in embryos injected with non-immune IgG or PBS. Increased expression of PCNA and decreased expression of neuronal class III beta-tubulin were observed in the spinal cord after anti-CL-PSP IgG injection. These results suggest that PSP controls the proliferation and differentiation of neuroepithelial cells in chick embryos.

Animals↗
PubMed1990

[Some chemical and serological properties of perchloric acid-soluble glycoproteins separated from ascitic fluid of a patient with metastatic omentum tumor from ovarian cancer].

One mol perchloric acid-soluble fraction (PASF) obtained from ascitic fluid of a patient (blood group B) with metastatic omentum tumor from ovarian cancer was a glycoprotein fraction containing 35.4% carbohydrate and exhibited A, B and Thomsen-Friedenreich (T) activities. This fraction was separated into three fractions, Frs. 1-3, by a gel filtration with Bio-Gel A-1.5 m column. Among these fractions, Fr. 1 which was obtained in a 5.5% yield to PASF, was a glycoprotein fraction with a high molecular weight, 23.3% carbohydrate and A, B and T activities. Other minor fraction, Fr. 2, and the major fraction, Fr. 3, contained 43.2% and 43.9% carbohydrate, but did not show A, B and T activities, respectively.

ABO Blood-Group System↗
PubMed1981

Acid soluble and insoluble glycogen in human skeletal muscle.

Quantitative biochemical analysis of glycogen was performed with and without perchloric acid pretreatment on biopsy specimens of varying glycogen content, obtained at rest and immediately after exercise after different diets. If analysis was carried out after perchloric acid pretreatment, as is commonly done, lower values were obtained than without such pretreatment. This could be explained by the existence of glycogen in forms of greater and lesser solubility. Evidence for this was obtained by quantitative analysis of glycogen in the perchloric acid extract. The acid soluble form in the extract constituted a greater fraction of total glycogen at supra-normal than at low concentrations. This might also explain why supra-normal levels of glycogen cannot be detected by histochemical methods. The existence of soluble and insoluble glycogen may also be of physiological importance, e.g. by interacting differently with enzymes of glycogen metabolism.

Adult↗
PubMed2003

Measurement of protein and lipid hydroperoxides in biological systems by the ferric-xylenol orange method.

Methods were developed for the separation and measurement of lipid and protein hydroperoxides, which can be used for biological materials. Lipids were extracted with methanol:chloroform and their hydroperoxides measured in solutions of methanol and chloroform containing 110mM perchloric acid, xylenol orange, and ferrous iron. Proteins were isolated by precipitation with 0.2M perchloric acid. The precipitates were redissolved in 6M guanidine hydrochloride and washed with chloroform, and the hydroperoxides were measured in the presence of perchloric acid, xylenol orange, and ferrous iron. Optimum conditions for hydroperoxide measurements were established and the assays were applied to oxidized human blood serum and to cultured cells.

Animals↗
PubMed1990

[Separation of Thomsen-Friedenreich (T) antigen and N antigen precursor glycoproteins from perchloric acid-soluble fraction of cyst fluid of human ovarian clear cell carcinoma and their some chemical and serological properties].

One M perchloric acid-soluble fraction separated from cyst fluid of a patient (blood group AB) with ovarian clear cell carcinoma in malignant was subjected to Sephacryl S-200 gel filtration and Fraction 1 which was eluted at void volume, reacted with both of the lectins of Vicia unijuga and Arachis hypogaea. This fraction was then separated into 6 fractions (DEAE-Frs. 1-6) in a DEAE-Sephacel column chromatography. DEAE-Frs. 3-6 were sugar-rich glycoprotein fractions which contained galactose and N-acetylglucosamine in remarkably high percentages, respectively. Reactivities against various hemagglutinins of these four fractions suggest that DEAE-Fr. 3 is a Thomsen-Friedenreich (T) glycoprotein fraction with AB activity and weak N antigen precursor activity and DEAE-Fr. 4 is an N antigen precursor glycoprotein fraction with AB activity and weak T activity.

Adenocarcinoma↗
PubMed2006

Perchloric acid-soluble protein is expressed in enterocytes and goblet cells in the intestine and upregulated by dietary lipid.

We previously identified perchloric acid-soluble protein (PSP) in the rat liver, kidney, brain and lung, and reported that it appeared to be related to repression of cell proliferation. In the present study, we clarified that PSP was expressed in the intestine, and found that the amino acid sequence of the intestinal PSP was consistent with those of other PSPs present in other tissues. An immunohistochemical study revealed that PSP was expressed in enterocytes and goblet cells, but not in other cell types among the lamina propria epithelial cells. A comparison of the expressions of PSP and proliferating cell nuclear antigen demonstrated that the proliferating cells did not express PSP. Intestinal PSP expression was induced by approximately 3-fold by oral administration of dietary fat. These findings indicate that the proliferation repression activity may be related to renewal of the intestinal epithelium, and that PSP is one of the fatty acid-inducible proteins.

Animal Feed↗
PubMed1975

Perchloric acid-soluble proteins and protein-bound hexoses in serum and tissues of normal, hypo-and hyperthyroid rats.

The total content of perchloric acid-soluble proteins (PCA-SP) and protein-bound hexoses (PBH) were studied in blood serum and tissues (liver, kidney, lung, brain) of normal, hypo- and hyperthyroid rats. The results obtained indicate that the hyperthyroid state induced an increase in both PCA-SP and PBH in blood serum and studied tissue homogenates, and hypothyreosis causes a decrease of total glycoproteins content in all studied materials. The results were counted per 1 g of protein and in this way the nonspecific effect of thyroid hormones on the protein metabolism had no influence on the measurements.

Animals↗
PubMed1977

Comparison of whole plasma and perchloric acid-extracted plasma assays for carcinoembryonic antigen.

A direct, paired, comparison was made of two plasma radioimmunoassays for carcinoembryonic antigen (CEA), between a perchloric acid-extracted, ammonium sulphate precipitation method; and a whole-plasma, double-antibody method. For both assays the same preparations of standard CEA, 125I-labelled CEA, and anti-CEA serum were used. Plasma samples were taken from young healthy subjects (24), cancer-free hospital inpatients (44) and cancer-proven untreated patients (94). Within-batch and between-batch variation were both greater for the extracted-plasma method. Cancer discriminatory ability was assessed by probabilistic means. With cancer-free inpatients as the reference group, no difference between the assay methods was revealed. With young healthy subjects as the reference group the whole-plasma assay was superior.

Adult↗
PubMed2000

Expression and cellular distribution of perchloric acid-soluble protein is dependent on the cell-proliferating states of NRK-52E cells.

To clarify the biological role of kidney perchloric acid-soluble protein 1 (K-PSP1), its expression and intracellular distribution were examined in normal rat kidney epithelial NRK-52E cells. K-PSP1 expression was low during the proliferating phase and high in the stationary phase, and shown to have a negative relationship with the protein-synthesizing activity of the cells. Immunocytochemical studies revealed that K-PSP1 is predominantly located in the cytosol, especially in endoplasmic reticulum and Golgi apparatus of proliferating cells. In the stationary phase, K-PSP1 was not detected immunologically even though protein and mRNA expression were high. This disappearance of reactivity with anti-serum seems to be due to a conformational change in K-PSP1 induced by unknown factors. These results suggest that the role of K-PSP1 is to regulate cell proliferation, and this may be related to a previously reported ability to inhibit protein synthesis.

Animals↗
PubMed1985

Proteinase inhibitors of horse seminal plasma. A high molecular mass, acid-soluble proteinase inhibitor.

Horse seminal plasma does not possess a proteinase inhibitor corresponding to human HUSI-I (human seminal plasma inhibitor). Instead a protein complex of high relative molecular mass (Mr) containing proteinase inhibitory activity was detected, which was called horse seminal plasma protein complex or HSPC. The compound had a broad enzyme-inhibiting spectrum. Its Mr was estimated to be 800 000 and it was composed of 7 different polypeptides with Mr values ranging from 11 000 to 30 000. Its carbohydrate content was between 3.5% and 5%. Despite the high molecular mass, the complex was soluble in diluted perchloric acid and did not lose its biological activity. The high recovery of seminal plasma protein (69%) after perchloric acid treatment, the unaltered immunoelectrophoretic precipitation pattern of the perchloric acid soluble part of seminal plasma, and the similarity of the polypeptide patterns of unfractionated seminal plasma and HSPC suggest that HSPC is one of the major components of horse seminal plasma. In addition to HSPC, horse seminal plasma contained a group of three electrophoretically distinguishable proteinase inhibitors, corresponding roughly to a Mr of 6500. They inhibited only trypsin. The similar Mr values and the identical narrow enzyme specificity suggest that they are isoinhibitors and may be analogues of human HUSI-II (human seminal plasma inhibitor). The lack of a HUSI-I analog in the horse is discussed in relation to a previously made observation that horse tracheobronchial fluid contains no detectable perchloric acid-soluble proteinase inhibitors.

Animals↗
PubMed1978

Determination of zirconium in natural water by spectrophotometry following the concentration step with yield tracer.

Zirconium in natural water samples was determined spectrophotometrically after concentration using95Zr as a yield tracer. Acidified sample (1l) with a known amount of 95Zr was evaporated to dryness, treated with hydrofluoric and nitric acids, and then with nitric and perchloric acids, and evaporated nearly to dryness. The residue was taken up with 2 M perchloric acid and zirconium in the solution was extracted with 0.1 M thenoyltrifluoroacetone (TTA) in benzene. The TTA complex solution was converted to hydrochloric acid solution. After the recovery yield was estimated by measuring the radioactivity of 95Zr in the final solution, zirconium was then determined by spectrophotometry with Arsenazo III. Zirconium contents in lake and hot and cold spring samples from Nikko and Shiobara districts were found to be 0.29-2.8 microgram/l by this method.

Fresh Water↗
PubMed2004

Upregulation of rat P23 (a member of the YjgF protein family) by fasting, glucose diet and fatty acid feeding.

In a previous study, we identified and purified a 99-amino-acid rat liver-kidney perchloric-acid-soluble 23-kDa protein (P23) which displays 30% identity with a highly conserved domain of heat shock proteins (HSPs), as well as an AT-rich 3' untranslated region, which has also been described to play a role in H70 mRNA life span and protein expression. An identical perchloric-acid-soluble protein inhibiting protein synthesis in a rabbit reticulocyte lysate system was also found 2 years later by another group. More recently, the novel, the YjgF, protein family has been described, comprising, 24 full-length homologues, including P23, highly conserved through evolution, and consisting of approximately 130 residues each and sharing a common ternary structure. Independent studies from different laboratories have provided various hypothetical functions for each of these proteins. The high degree of evolutionary conservation may suggest that these proteins play an important role in cellular regulation. Although the function of none of these proteins is known precisely, we present experimental evidence which, combined with the relationship to glucose-regulating protein revealed here, and the relationship to fatty-acid-binding protein revealed by others, allow us to propose a role for P23. In rat liver, P23 expression is developmentally regulated and modulated by dietary glucose, and its mRNA is induced by starvation, in the presence of fatty-acids and in 3-MeDAB-induced hepatomas. The mRNA encoding mouse liver P23 is also hormonally modulated in a mouse line AT1F8. These data indicate that P23 protein might be a key controller of intermediary metabolism during fasting.

Animals↗
PubMed2003

Liquid chromatography for iothalamate in biological samples.

We have previously reported an iothalamate assay for the assessment of the glomerular filtration rate (GFR) that required a long column equilibration time and 22 min run time per sample. We now report a simpler assay that requires a run time of only 5.5 min and is more precise and accurate than the earlier technique. The mobile phase consisted of methanol-acetonitrile-50 mM sodium monobasic phosphate (10:5:85, v/v) at pH 4.4, pumped at a rate of 1.5 ml/min on a C(18) reversed-phase column. Samples of plasma and urine were deproteinized with 1 volume of 4% perchloric acid or 9 volumes of 2% perchloric acid, respectively. No internal standard was used. The diode array detection system collected absorbance at 240 nm and the peak height areas of iothalamate were determined. The iothalamate peak appeared at 3.5 min. Detector response was linear over the range tested (10-2000 microg/ml). Within-run precision was <3% for both plasma and urine and accuracy was 96-102%. Between-day precision for plasma and urine analyses were <7%. The recovery of iothalamate in urine and plasma were 102% and 91%, respectively. There was excellent thermal and pH stability of iothalamate. No interference was found with para-amino hippuric acid (PAH) or N-acetyl PAH, which can be simultaneously assayed, if desired.

Adolescent↗