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)

Prolactin and alpha-1,4-glucosidase levels in seminal plasma were measured in poorly coagulated (I), deficiently coagulated (II) and normally coagulated (III and IV) human ejaculates having 0-20%, 21-50% and 51-100% coagulum respectively 4 min after emission. The prolactin concentration (ng ml-1, mean +/- SEM) in poorly coagulated (5.2 +/- 0.48) and deficiently coagulated (7.6 +/- 0.72) samples was significantly lower than in the normally coagulated groups III (51-75% coagulum, 8.2 +/- 0.43) and IV (76-100% coagulum, 9.9 +/- 0.59) as well as the presumably fertile samples (9.2 +/- 0.74). A highly significant positive correlation was observed between the prolactin level and the percentage coagulum of the ejaculates (r = 0.686, n = 58, P less than 0.001). In contrast, the epididymal marker, alpha-glucosidase showed no relationship to seminal coagulation.
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PMID:Prolactin and alpha-1,4-glucosidase activity in normal and poorly coagulated human semen. 206 61

Prolactin proteolysis by rat pituitary homogenates was assayed by measuring the release of trichloroacetic acid-soluble peptides from 125I-labelled rat prolactin. There was a distinct optimum at pH 4.3, with only trace amounts of activity at neutral and alkaline pH. Rat pituitary homogenates were subjected to analytical subcellular fractionation by sucrose density gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their respective marker enzymes, including: cytosol (lactate dehydrogenase); plasma membrane (5'-nucleotidase); lysosomes (N-acetyl-beta-glucosaminidase, beta-glucuronidase); mitochondria (particulate malate dehydrogenase); endoplasmic reticulum (neutral alpha-glucosidase); prolactin granules (radioimmunoassayable prolactin). Acid prolactin protease had a similar distribution to the lysosomal marker enzymes. A localisation of the activity to lysosomes was confirmed by subcellular fractionation experiments in which the lysosomes were selectively disrupted with low concentrations of the membrane perturbant, digitonin. Experiments with specific inhibitors of the lysosomal cathepsins indicate that both cathepsins B and D are implicated in pituitary prolactin proteolysis.
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PMID:Analytical subcellular fractionation of rat pituitary homogenates, with special reference to prolactin proteolysis by lysosomes. 729 6

The growth and maturation of the gastrointestinal tract during development is influenced by diverse genetic and growth factors. Since prolactin is abundant in amniotic fluid and breast milk, we hypothesized that it may also affect gut development. The effect of prolactin on thymidine incorporation and tissue alkaline phosphatase, maltase and lactase activity was studied on jejunal explants from fetal, newborn and 2 week-old rats. The results were compared with the effects of epidermal growth factor (EGF) under identical experimental conditions. Prolactin induced a significant increase in proliferation and a two- to threefold increase in maltase and alkaline phosphatase activity of the newborn explants. The effect of prolactin in this group compared to that of EGF was significantly greater with respect to proliferation, and almost identical with respect to the hydrolases studied. These results suggest that prolactin might have a role in the process of growth and maturation of the gut mucosa during ontogeny.
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PMID:A possible role of prolactin on growth and maturation of the gut during development in the rat. 1209 87