Identification of a calcium-dependent microsomal proteinase responsible for monobasic cleavage of chicken proalbumin.
The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(-1)----Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant alpha 1-antitrypsin Pittsburgh, but not by normal alpha 1-antitrypsin.
Peach
R J
RJ
Pathology Department, Christchurch School of Medicine, New Zealand.
Brennan
S O
SO
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000502:physiology*; D002645:Chickens; D002648:Child; D010450:Endopeptidases / Q000502:physiology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000302:isolation & purification / Q000378:metabolism*; D012709:Serum Albumin / Q000302:isolation & purification
D011228:Prealbumin; D012709:Serum Albumin; D010450:Endopeptidases; D002118:Calcium