Enzymatic maturation of pro-opiomelanocortin by anterior pituitary granules. Methodological approach leading to definite characterization of cleavage sites by means of high-performance liquid chromatography and microsequencing

Autor: N G, Seidah, D, Pélaprat, J, Rochemont, P, Lambelin, M, Dennis, J S, Chan, J, Hamelin, C, Lazure, M, Chrétien
Rok vydání: 1983
Předmět:
Zdroj: Journal of chromatography. 266
Popis: The coupling of high-performance liquid chromatography, gel-permeation, and reversed-phase chromatography with microsequencing proved to be advantageous for the unambiguous determination of specific sites in pro-opiomelanocortin, cleaved by secretory granule lysates of pig anterior pituitary. This system allows the unambiguous identification of a major chymotrypsin-like enzyme activity, optimal at pH 8.0, in the granule preparation, with a specificity directed towards some Phe decreases X and Tyr decreases X cleavage sites. The approach used emphasizes the necessity to use methodologies leading to the unambiguous determination of conversion activities.
Databáze: OpenAIRE