Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat intestinal maltase-glucoamylase was purified in the presence of detergent and proteolytic inhibitors, and the 130000 and 145000 subunits were separated and isolated by preparative sodium dodecyl sulfate - polyacrylamide gel electrophoresis and electrophoretic elution. Amino acid analyses were very similar, with a small excess of apolar amino acid residues in the 145000 subunit. Peptide mapping with Staphylococcus aureus V8 protease revealed eight similar peptide products for each, with apparent elongation of the five larger peptides in the 145000 subunit by a relative mass (Mr) of 2000-5000. alpha-Chymotrypsin maps showed at least eight identical cleavage products plus one large, shared product which was larger by a Mr of 5000 in the 145000 subunit. Cyanogen bromide cleavage of the 145000 subunit produced a single peptide of Mr 75000. A peptide of Mr 66000, also indicative of a central cleavage, was generated from the 130000 subunit, but a second cleavage into 43000 and 23000 segments was also evident. Several sets of antibodies formed against both antigens consistently gave reactions of identity without spurring on immunodiffusion. These results indicate extreme homology between the central segment of the 145000 subunit and the 130000 subunit. The cyanogen bromide cleavage results suggest, however, that the two central sequences are not absolutely identical and therefore that one subunit may not be a posttranslational derivative of the other.
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PMID:Mapping of proteolytic and cyanogen bromide peptides from subunits of intestinal maltase-glucoamylase: evidence for significant homology. 392 86

To determine whether incorporation of peptides into diets can improve larval development, sea bass (Dicentrarchus labrax) larvae were fed for 21 d one of three isonitrogenous, isoenergetic semipurified diets in which enzymatic hydrolysate (75% di- and tripeptides) of fish meal proteins was substituted for 0, 20 or 40% of native fish meal proteins. Growth and survival were significantly greater (P < 0.05) in larvae fed peptide diets compared to those fed only native protein, with the best performance exhibited by those fed the 20% level of peptides. Chymotrypsin activity was much higher in groups fed peptide diets compared to that fed all native protein (P < 0.001), indicating a greater proteolytic capacity of the pancreas. At the intestinal level, activities of the brush border enzymes, aminopeptidase, maltase and gamma-glutamyl transpeptidase, increased with age while the cytosolic enzyme, leu-ala peptidase, decreased with age (P < 0.001). These changes in enzymatic activities correspond to the normal development of intestinal digestion. This development occurred earlier in the group fed 20% peptide-substituted diet than in the two other groups. The better larval performances observed in groups fed diets containing peptides can be related to the enhanced proteolytic capacity of the pancreas and the earlier development of intestinal digestion.
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PMID:Partial substitution of di- and tripeptides for native proteins in sea bass diet improves Dicentrarchus labrax larval development. 910 12

To evaluate the effect of chymotrypsin on the examination of alpha-glucosidase activity in seminal plasma, thirty-nine samples of fresh liquefied semen with or without chymotrypsin and forty-eight samples of fresh un-liquefied semen with chymotrypsin were determined for the total alpha-glucosidase activity in seminal plasma. The total alpha-glucosidase level of each sample was assayed by the method of glucose oxidase. The correlations between alpha-glucosidase level and semen parameters, including semen volume, pH, sperm concentration, grade a and b motility and total motility, were analyzed with SPSS 11.0 software. The results showed that chymotrypsin had no effect on seminal alpha-glucosidase activity determination. Chymotrypsin could improve the liquefaction for un-liquefied semen, and there was no significant difference of alpha-glucosidase activity between liquefied and un-liquefied semen samples. There were significantly positive correlations between seminal alpha-glucosidase activity (U/ml) and sperm concentration (r = 0.338, p = 0.015) and between total alpha-glucosidase activity (U/ejaculate) and semen volume (r = 0.677, p = 0.000). However, there was no significant correlation between alpha-glucosidase level (U/ml) and semen volume, pH, sperm motility or grade a and b motility (r = -0.234 approximately 0.077, p = 0.099 approximately 0.993). The data indicated that chymotrypsin could be added into the un-liquefied semen samples for alpha-glucosidase activity determination, and there were different correlations between seminal alpha-glucosidase level and various semen parameters.
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PMID:The effect of chymotrypsin on the determination of total alpha-glucosidase activity in seminal plasma and the correlation between alpha-glucosidase level and semen parameters. 1705 Mar 25