Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Development of the synthesis and secretion of gastric proteases was studied in 55 Large White x Landrace pigs from 22 days before birth (93 days gestation) to 36 days of age. The pigs came from eight litters and were 0.4 - 13.5 kg body weight. Littermate pairs were treated with either saline or adrenocorticotropin (ACTH) from three days of age. Secretion of protease activity (milk-clotting and general proteolytic activity) was investigated in anaesthetized pigs by a gastric perfusion technique using intravenous infusion of pentagastrin at dose rates of 4 and 8 micrograms/h per kg body weight. In addition, concentrations of protease zymogens (prochymosin, pepsinogen A, progastricsin) were measured in fundic tissue extracts by rocket immunoelectrophoresis. Prochymosin was present in fundic tissue at 22 days before birth, reached peak concentrations at birth and decreased in concentration during the subsequent 36 days. Pepsinogen A and progastricsin were absent or present in trace amounts in the first week after birth, but thereafter concentrations of both zymogens increased rapidly. Development of the pentagastrin-stimulated secretion of protease activity reflected the changes of zymogen concentrations in fundic tissue. Chronic treatment of pigs with ACTH from three days of age significantly increased the concentration of prochymosin in fundic tissue at 9-11 days and the concentrations of pepsinogen A and progastricsin at 34-36 days of age. Hormones such as ACTH and glucocorticoids may therefore play a regulatory role in the ontogeny of porcine gastric proteases.
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PMID:Development of gastric proteases in fetal pigs and pigs from birth to thirty six days of age. The effect of adrenocorticotropin (ACTH). 166 4

Purification of pepsinogen B from dog stomach was achieved. Activation of pepsinogen B to pepsin B is likely to proceed through a one-step pathway although the rate is very slow. Pepsin B hydrolyzes various peptides including beta-endorphin, insulin B chain, dynorphin A, and neurokinin A, with high specificity for the cleavage of the Phe-X bonds. The stability of pepsin B in alkaline pH is noteworthy, presumably due to its less acidic character. The complete primary structure of pepsinogen B was clarified for the first time through the molecular cloning of the respective cDNA. Molecular evolutional analyses show that pepsinogen B is not included in other known pepsinogen groups and constitutes an independent cluster in the consensus tree. Pepsinogen B might be a sister group of pepsinogen C and the divergence of these two zymogens seems to be the latest event of pepsinogen evolution.
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PMID:Primary structure, unique enzymatic properties, and molecular evolution of pepsinogen B and pepsin B. 1214 55