Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During the mating reaction between mt+ and mt- gametes of Chlamydomonas reinhardtii, two novel endopeptidases, each of which was able to digest the B chain of insulin, were released into the culture medium, together with a gamete lytic enzyme (GLE) which is responsible for digestion of the gametic cell walls. Both endopeptidases and GLE were copurified from the mating medium by column chromatography on DEAE-cellulose and concanavalin A. Gel filtration separated the peptidases, which were unable to digest gametic cell walls, into two fractions, endopeptidase-1 and endopeptidase-2. These enzymes were also separated from GLE, which was unable to digest the B chain of insulin. Endopeptidase-1, with a molecular mass of about 200 kDa, cleaved the B chain of insulin at the Ala14-Leu15 peptide bond, and this activity was inhibited by EDTA. Endopeptidase-2, with a molecular mass of about 110 kDa, digested the peptide at the Leu15-Tyr16 peptide bond and was sensitive to iodoacetate and chymostatin. When the cell walls of gametes of either mating-type were digested prior to mating with exogenously added GLE, the two endopeptidases were released into the medium, a result that suggests that they are stored, like GLE, outside the plasmalemma.
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PMID:Two novel endopeptidases released into the medium during mating of gametes of Chlamydomonas reinhardtii. 798 65

Proteolytic hydrolysis rates of neurotensin and acetyl-neurotensin-(8-13) by brush-border membranes from various rat intestinal segments were as follows: jejunum > duodenum approximately jejunoileal junction > ileum > caecum. The rank order of endopeptidase-24.11 activity along the intestine was jejunum > duodenum approximately jejunoileal junction > ileum > caecum. Angiotensin converting enzyme (ACE) had a similar distribution profile as endopeptidase-24.11. Activities of these two enzymes were lower in the distal intestine. Distribution of endopeptidase-2 activity along the intestine was different: ileum > duodenum approximately jejunum approximately jejunoileal junction > caecum. The profiles of differential hydrolysis of neurotensin and acetylneurotensin-(8-13) within the gut corresponded to the distribution of endopeptidase-24.11 and ACE. Moreover, effects of enzyme inhibitors confirm that these two enzymes initiated proteolysis of neurotensin and acetylneurotensin-(8-13). These results suggest that the regional differences in the activities of key brush-border membrane peptidases will affect site-dependent stability of peptide drugs.
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PMID:Influences of regional differences in activities of brush-border membrane peptidases within the rat intestine on site-dependent stability of peptide drugs. 841 76


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