Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00631 (Gel)
 14,881 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An enzyme extract from Cellulase-Onozuka, a commercial product of Trichoderma viride, was fractionated by Amberlite CG-50 column chromatography into three cellulase [EC 3.2.1.4] groups, peaks I to III. A noval enzyme, which has both beta-glucosidase [EC 3.2.1.21] and exo-carboxymethyl-cellulase (exo-CMCase) properties was obtained from peak III by extensive purification throuh consecutive column chromatography. The enzyme was homogeneous on ultracentrifugation, SDS-gel and cellulose acetate film electrophoreses and molecular sieve chromatography on Bio-Gel P-150. The molecular weight of this enzyme was estimated to be 53,000. The enzyme appeared to release cellobiose residues one by one from the nonreducing end of higher cellooligosaccharides and CM-cellulose (CMC), but to release glucosyl residues from reduced cellotriose and beta-cellobioside, resembling a beta-glucosidase in this respect. Furthermore, this exo-CMCase also attacked xylan exo-wise to produce xylobiose moleculaes one by one, but it scarcely attacked insoluble cellulose, except for a cellodextrin apparently rich in amorphous structure.
J Biochem 1975 Sep
PMID:Purification and properties of an exo-cellulase component of novel type from Trichoderma miride. 0 9

The "oxytocinase" activity has been determined as the CAP (cystyl-aminopeptidase, EC 3.4.11.3) activity with several substrates. It was demonstrated that serum samples from pregnant women and patients with serious liver disease had increased CAP activities compared with normal serum. It was also shown that seminal plasma had very high CAP activity. The pH optimum for the enzymes from the various sources differed, as did the metal dependence. Furthermore, samples from patients with liver disease had higher CAP activities when assayed in buffers containing amino groups, in contrast to the other samples. Gel chromatography and gel electrophoresis revealed the presence of several isoenzymes. The serum from pregnant women contained an isoenzyme neither present in normal plasma nor in any of the other sources tested. It is possible that this isoenzymes represents the true oxytocinase. CAP and LAP (leucine aminopeptidase) activities were very well correlated in serum from pregnant women and seminal plasma, while the correlation for samples from patients with liver disease was not as good. When care was taken to determine the CAP activity at the right pH and with the appropriate buffer, the risk for interference from other enzymes was minimized in the determination of oxytocinase as CAP activity.
Clin Chim Acta 1978 Sep 01
PMID:Determination of cystyl-aminopeptidase. Isoenzymes in seminal plasma and serum of different origin. 2 26

Gel chromatography on Sepharose and on Sephadex was used to separate the soluble phenol oxidase in various potato juices into multiple molecular forms ranging from 36,000 to 800,000 daltons. Adjustment of potato juice from physiological pH (ca. 6) to pH 4.5 or to pH 7.8 resulted in the predominance of low-mol.-wt. (less than 150,000 daltons) or high-mol.-wt. (greater than 150,000 daltons) enzyme forms, respectively. This suggests association phenomena of subunits. In potato juice of physiological pH and in potato juice adjusted to pH 4.5, all enzyme forms exhibited both monophenol and o-diphenol oxidase activities (assayed at pH 6.0). In potato juice adjusted to pH 7.8 considerable loss of monophenol oxidase activity (assayed at pH 6.0) occurred. This suggests that o-diphenol oxidase is more alkali-stable than monophenol oxidase. The significance of these findings for enzyme purifications and for the in vivo action of the enzyme is discussed.
Z Lebensm Unters Forsch 1979 Sep
PMID:Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen oxidoreductase (EC 1.14.18.1) from potato tubers (Solanum tuberosum). III. Influence of pH on the molecular weight distribution of enzyme activity in potato juice. 4 78

Mouse immune (type T) interferon was produced from suspensions of spleen cells (1 X 10(7) cells/ml) treated with 3 micrograms/ml of phytohaemagglutinin. The crude interferon was chromatographed on four sorbents with varying affinities, namely concanavalin A-Sepharose, Affi-Gel 202, Blue Sepharose CL-6B and Phenyl-Sepharose CL-4B. With each of these the interferon activity was observed to have considerable heterogeneity. By means of affinity chromatography, mouse immune interferon was purified 100 to 200 times with concomitant complete recovery of activity.
J Gen Virol 1979 Sep
PMID:Physico-chemical characterization and partial purification of mouse immune interferon. 4 58

Growth hormone release-inhibiting hormone (somatostatin), a hypothalamic peptide that inhibits the release of growth hormone and also the secretion of insulin glucagon, and gastrin, was found in the rat stomach and pancreas in a concentration similar to that in the hypothalamus, as measured by radioimmunoassay. Somatostatin was also found in the duodenum and jejunum, but in a smaller concentration. Gel filtration of the extracts of the pancreas and stomach on Sephadex G-25 yielded two immunoreactive peaks, one corresponding in each case to the somatostatin tetradecapeptide. The hormone was not detected in other viscera or the ovaries. The results imply that somatostatin may be synthesized in the pancreas and the stomach in addition to the brain, and may be involved in local regulatory mechanisms for pancreatic and gastric secretion as well as secretion of growth hormone.
Science 1975 Sep 19
PMID:Somatostatin: abundance of immunoreactive hormone in rat stomach and pancreas. 5 79

Foot-and-mouth disease virus (a member of the picornavirus group) RNA could be translated effectively in an S-30 extract from Ehrlich ascites tumour cells. This translation was inhibited by aurintricarboxylic acid, cycloheximide, puromycin and RNase. Cell-free products of translation were identified by disc gel electrophoresis and immunoprecipitation with specific antisera. Gel electrophoresis of the products without prior immunoprecipitation suggested the synthesis of some of the non-capsid proteins and capsid proteins VP1, VP2 and VP3 of the virus. Immunoprecipitations with antisera against whole virus and VP3 indicated the synthesis of VP3 and of at least two additional peptides of 100 000 and 56 000 daltons containing antigenic sites of VP3. Gel electrophoresis after immunoprecipitation with antiserum against virus infection-associated antigen indicated the synthesis of a different 56 000-dalton protein appearing to resemble non-capsid protein NCVP5. The amount of foot-and-mouth disease virus and VP3-specific peptides in the virus RNA-directed products were measured by immunoprecipitation.
J Gen Virol 1976 Sep
PMID:Cell-free translation of foot-and-mouth disease virus RNA into identifiable non-capsid and capsid proteins. 6 Dec 50

Colon-specific antigen-p, or CSAp, was originally extracted from GW-39 tumors, which are human colonic carcinomas serially transplanted in golden hamsters, and antibodies to CSAp have been produced in the same animal hosts. By means of immunodiffusion and a hemagglutination-inhibition assay, CSAp has been found to be restricted to adult and fetal small intestine, neoplastic gastric and colonic tissues, inflamed colon, and cystic mucinous tumors of the ovary. CSAp was shown to be distinct from blood group antigens, including Lea and Leb blood group substances, liver ferritin, AFP, CEA, CSA, CMA, ZGM, and BOFA, and to have the electrophoretic mobility of an alpha2-globulin. Gel filtration studies indicated that CSAp in GW-39 tumor, primary human colonic carcinoma, and ovarian cancer mucinous cyst fluid had a peak molecular size range of 70,000--110,000. Quantitation of CSAp in 214 tissue specimens by the hemagglutination-inhibition assay revealed a progressive increase in fetal, inflamed, and neoplastic intestine, such that CSAp in colonic tumors was increased over normal colon tissue. Thus, CSAp appears to be an organ-specific antigen showing increased levels in some gastrointestinal and ovarian neoplasms, as well as in specimens with colitis.
Cancer 1978 Sep
PMID:Further characterization of CSAp, an antigen associated with gastrointestinal and ovarian tumors. 8 13

Bovine AFP was purified by ion exchange chromatograph on C.M. cellulose and DEAE Sephadex A-50, gel filtration and immunosorbent technique. AFP was homogeneous when studied by gel electrophoresis under non denaturing and denaturing conditions, by ultracentrifugation and by immunological methods. The following molecular data were obtained: 1. Sedimentation equilibrium indicated a molecular weight of 66,500 and sedimentation velocity gave s degrees 20, w = 4.71 S. A partial specific volume v = 0.737 ml g-1 was derived from density measurements. 2. From these data, a Stokes radius of 3.26 nm, a diffusion coefficient D20 w = 6.61 10(-7) cm2 sec-1 and a frictional ratio f/fo = 1.21 were calculated. 2. Sodium dodecylsulphate disc electrophoresis suggests a molecular weight of 67,000. 3. Gel filtration pointed to a molecular weight of 75,000. 4. Microheterogeneity of AFP was demonstrated by isoelectric focusing. The isoelectric point of the major component is 4.6. 5. The chemical composition was determined. AFP is a glycoprotein containing 7 per cent carbohydrate including 1.67 per cent hexoses, 2.38 per cent N-acetyl glucosamine and 1.8 per cent N-acetyl neuraminic acid.
Biochimie 1978 Sep 29
PMID:Bovine alpha-fetoprotein. Isolation and characterization. 8 53

Proteoglycans were extracted, in a yield of about 90%, from costal cartilage of young, growing guinea-pigs. Three solvents were used in sequence: 0.4 M guanidine - HCl, pH 5.8, 4 M guanidine - HCl, pH 5.8, and 4 M guanidine - HCl/0.1 M EDTA, pH 5.8. The proteoglycans were purified and fractionated by cesium chloride density gradient ultracentrifugation under associative and dissociative conditions. Gel chromatography on Sepharose 2 B of proteoglycan fractions from associative centrifugations showed the presence of both aggregated and monomer proteoglycans. The ratio of aggregates to monomers was higher in the second extract than in the other two extracts. Dissociative gradient centrifugation gave a similar distribution for proteoglycans from all three extracts. Thus, with decreasing buoyant density there were decreasing ratios of polysaccharide to protein, and of chondroitin sulfate to keratan sulfate. In addition, there was with decreasing density an increasing ratio of chondroitin 4-sulfate to chondroitin 6-sulfate. Amino acid analyses of dissociative fractions were inaccordance with previously published results. On comparing proteoglycan monomers of the three extracts, significant differences were found. Proteoglycans, extracted at low ionic strength, contained lower proportions of protein, keratan sulfate, chondroitin 6-sulfate and basic amino acids than those of the second extract. The proteoglycans of the third extract also differed from those of the other extracts. The results indicate that the proteoglycans of guinea-pig costal cartilage exist as a very polydisperse and heterogenous population of molecules, exhibiting variations in aggregation capacity, molecular size, composition of protein core, degree of substitution of the protein core, as well as variability in the type of polysaccharides substituted.
Eur J Biochem 1975 Sep 15
PMID:Proteoglycans of guinea-pig coastal cartilage. Fractionation and characterization. 12 59

Factors with growth hormone and lactogenic activities have been identified in serum samples and placental extracts of 9 species using a radioreceptor assay for prolactin or lactogens (RRA-PRL) and one for growth hormone-like activity (RRA-GH). The concentrations of placental lactogen (PL) and growth hormone-like activity (GHLA) in pregnancy were different in each species. The levels of PL began to rise at or before mid-pregnancy and either remained elevated until term (hamster, goat, sheep, monkey, and human), declined gradually after reaching peak concentrations just beyond mid-pregnancy (guinea pig), or had 2 peaks of activity (mouse, rat). The peak concentrations in different species ranged from 350 ng/ml in the cow to 45,000 ng/ml in monkey serum samples. The concentrations of GHLA were similar to PL levels in the guinea pig, goat, cow, and monkey but were lower than PL levels in the sheep and human. The maximal concentrations of PL and GHLA in placental extracts varied from 1 mug/g in guinea pigs to 200 mug/g in sheep. The ratio of lactogenic/growth hormone-like activity of both serum and placental extracts varied greatly among the various species. Gel filtration studies of serum samples revealed that PL and GHLA in the hamster, mouse and rat had different elution volumes, whereas, in the remaining species, the two activities co-eluted.
Endocrinology 1976 Sep
PMID:Lactogenic and growth hormone-like activities in pregnancy determined by radioreceptor assays. 18 67


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