ACTION OF NEUROHYPOPHYSEAL GRANULE LYS-ARG ENDOPEPTIDASE ON SYNTHETIC POLYPEPTIDES COMPRISING THE PROCESSING SEQUENCE OF PROVASOPRESSIN-NEUROPHYSIN

被引:3
作者
MICHEL, G [1 ]
ROUILLE, Y [1 ]
CHAUVET, J [1 ]
ACHER, R [1 ]
机构
[1] UNIV PARIS 06,BIOL CHEM LAB,F-75006 PARIS,FRANCE
关键词
GRANULE LYS-ARG ENDOPEPTIDASE; NEUROHYPOPHYSEAL GRANULES; VASOPRESSINYL-PEPTIDE PROCESSING;
D O I
10.1007/BF01200246
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Neurohypophysial granule Ca2+-dependent endopeptidases have been allowed to act on synthetic polypeptides derived from the N-terminal sequence of bovine provasopressin-neurophysin, namely vasopressinyl-glycyl-lysyl-arginyl-alanylamide and vasopressinyl-glycyl-lysyl-arginyl-alany-methionyl-serinamide. Membrane-bound enzymes have been used at pH5.5 for 16 hr at 37 degrees C. Products have been identified by high-pressure liquid chromatography (HPLC) and by mass spectrometry performed on substances isolated by HPLC. With both substrates, vasopressinyl-Gly-lys-Arg(OH) has been identified as a product confirming the Lys-Arg specificity previously observed an small peptide fluorogenic substrates. Cleavage yields, however, appear low suggesting that some factors are missing, for example a targeting action of the precursor neurophysin domain to the granule membrane.
引用
收藏
页码:171 / 178
页数:8
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