Evidence that glycosylation of pro-opiocortin and ACTH influences their proteolysis by trypsin and blood proteases
作者： Y.Peng Loh , Harold Gainer
DOI: 10.1016/0303-7207(80)90092-1
关键词: Tunicamycin 、 Proteases 、 Trypsin 、 Adrenocorticotropic hormone 、 Proteolysis 、 Glycoprotein 、 Biochemistry 、 Glycosylation 、 Biology 、 In vitro 、 Molecular biology 、 Endocrinology
摘要: The role of the carbohydrate in stabilizaion and protection glycoprotein, pro-opiocortin, from non-specific proteolysis by trypsin blood proteases was studied vitro. [3H]Arginine-labeled, glycosylated non-glycosylated forms pro-opiocortin were isolated frog neurointermediate lobes subjected to trypsin. form degraded more rapidly than form. Analysis tryptic products after treatment, showed that cleaved unidentified peptides within 1 min, whereas prohormone yielded 2 products, mol. wt. 23 000 ACTH 21 ACTH, synthesized intact lobe. These data provide direct evidence support hypothesis, derived studies on lobe (Loh Gainer, 1978, 1979) glycosylation is important: (1) protect it against situ, (2) processing limiting proteolysis. In addition, we demonstrate are much stable forms.
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