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Biomedical subjects

G S Gupta

Publications and source records attributed to G S Gupta.

At least 73 records · Page 4Linked to original sources
PubMed1983

Isolation and characterization of the major form of beta-glucuronidase from human seminal plasma.

Human seminal plasma contain two forms of beta-glucuronidase (beta-D-glucuronidase glucuronosohydrolase, EC 3.2.1.31) which are present in the ratio of 4:1. The major form of beta-glucuronidase with a slow moving band in electrophoresis was purified to homogeneity as revealed by polyacrylamide gel electrophoresis, double immunodiffusion and immunoelectrophoresis. The major form of beta-glucuronidase shows dual optimum pH at 4.3 and 4.7 with a dip in the activity at pH 4.5. The Km of this form of beta-glucuronidase is dependent on pH and was found to be 0.95, 3.08 and 0.67 mM at pH 4.4, 4.5 and 4.7, respectively. The major form of beta-glucuronidase from seminal plasma is stable at 55 degrees C for 30 min but it denatures at 65 degrees C. Heat denaturation is faster at acidic pH (4.7) than at alkaline pH (7.8). However, the activity of enzyme increased linearly with increase in temperature up to 70 degrees C during incubation with substrate. Cu, Ag, Hg and Ni salts inhibited enzyme activity significantly at 0.1 and 1.0 mM concentration, but the inhibition of HgCl2 was protected by cysteine. 1,4-D-Saccharic acid lactone and ascorbic acid inhibited seminal beta-glucuronidase competitively, yielding Ki values of 1.7 . 10(-3) mM and 10.3 mM, respectively. Though fructose and mannose also showed significant inhibition of beta-glucuronidase at 10-100 mM, glucose did not show any effect. The molecular weight of the major form of beta-glucuronidase was found to be 279 000, and it appears to be composed of four subunits each having a molecular weight of 74 000.

Chromatography, Gel↗
PubMed1982

Immunoenzymic studies on testicular hyaluronidase from rhesus monkeys (Macaca mulatta).

Hyaluronidase from rhesus monkey testes was purified by detergent extraction, ammonium sulphate fractionation, Sephadex G-200 column chromatography and concanavalin A-Sepharose affinity chromatography. The purified hyaluronidase showed one protein band on acrylamide gel electrophoresis. Antibodies to the purified hyaluronidase were raised in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. The enzyme had a molecular weight of 62,000. The Km was 0.5 mg/ml for hydrolysis of hyaluronic acid at 37 degrees C. The optimum pH for the enzyme was 5.0 but activity was present over a broad pH range. The hyaluronidase was inhibited by HgCl2, CuSO4, FeSO4 and p-chloromercuribenzoate all at a concentration of 2 x 10(-4) M. Cysteine protected the enzyme against HgCl2 inhibition.

Animals↗
PubMed1981

Isolation, properties, immunological specificity and localization of mouse testicular hyaluronidase.

Hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35) was purified from mouse testes by ion-exchange chromatography, Sephadex G-200 filtration and Con A-agarose affinity chromatography. The final preparation had 94-fold purity and 12.2 units spec. act. of the enzyme (unit of specific activity = mumol N-acetylglucosamine released/h per mg protein at 37 degrees C and pH 4.5). Hyaluronidase is relatively heat stable and loses 10-20% of its activity at 50-55 degrees C for 10 min. Ea for eat denaturation of enzyme is 42-45 kcal between 45 an 63 degrees C. The Michaelis constant of mouse testicular hyaluronidase is 1.1 mg/ml hyaluronic acid. Antibodies to the purified enzyme were produced in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. Antiserum to hyaluronidase inhibited enzyme activity by 25%. Immunologically, mouse testicular hyaluronidase is species specific. Tissue extracts of mouse vital organs, except testes and epididymis did not react with the antisera, though nonspecific precipitation occurred between intestinal extracts and anti-hyaluronidase serum. Hyaluronidase was localized in testis sections by indirect immunofluorescence. A specific dark green fluorescence was localized on cell boundaries extending from spermatogonia to spermatids and appeared on the sperm acrosome. Cytoplasm of spermatogonia and spermatocytes showed light green fluorescence, whereas interstitial tissue was devoid of fluorescence.

Animals↗
PubMed1981

The acute toxicity of endosulfan to fresh-water organisms.

A static bioassay is performed for measuring the short-term (96 h) toxicity of endosulfan to juvenile catfish Clarias batrachus, insect nymph Enallagma sp. and frog tadpoles of Rana tigrina. Median Tolerance Limit, Slope Function, Confidence Limit, and Presumable Harmless Concentration were computed. The results showed that frog tadpoles are more susceptible to endosulfan than insect nymph and catfish. Morphological changes and behavioural alterations were evaluated as symptoms of endosulfan toxicity.

Animals↗
PubMed1980

Biological damage in spleen by iodine-125 in potassium perchlorate blocked thyroid of rats.

Studies on spleen have been performed following administration of iodine-125 in perchlorate-treated rats. Although DNA levels did not change appreciably, there was a significant decrease in total RNA following incorporation of iodine-125. Associated with the changes in RNA, there was a significant rise in acid phosphatase and total as well as Mg-dependent ATPases. Increased activity of acid phosphatase seems to be related to the loss of lymphocytes, whereas the rise in ATPase appeared to be associated with cells of red pulp of spleen. It is suggested that damage to the spleen after administration of iodine-125 is due to the Auger effect.

Acid Phosphatase↗
PubMed1980

Effect of endosulfan of bioelectrical activity of brain in rats.

Bioelectrical activity of rat brain was studied after administration of endosulfan (5 mg/kg, ip) for 10 days. The pesticide produced rhythmic bursts of spikes and waves of seizure pattern that started 25-30 minutes after dosing and persisted for 60-minutes. The clonic convulsions were more marked over the head region and were mainly localized in the upper extremities. Histopathologic examination of the liver showed congestion of the central veins and its adjacent sinusoids. Concentration of the compound in brain parallelled the electrical activity.

Animals↗