Purification and characterization of angiotensin II-generating chymase from hamster cheek pouch.
Hamster cheek pouch vascular tissues contain an angiotensin II-forming enzyme which is inhibited by chymostatin but not by any angiotensin-converting enzyme inhibitors. The enzyme was purified to apparent homogeneity by gel filtration and heparin-Sepharose affinity chromatography. The molecular mass estimated by sodium dodecyl sulphate polyacrylamide gel electrophoresis was 28 kDa and the optimum pH was between 7.5 and 9.0. The angiotensin II-forming activity was inhibited by chymostatin, soybean trypsin inhibitor and phenylmethylsulfonyl fluoride, but not by aprotinin. The N-terminal sequence showed high homology with chymases from various species. Thus, the angiotensin II-generating enzyme obtained from hamster cheek pouch vessels is a chymase.
Takai
S
S
Department of Pharmacology, Osaka Medical College, Japan.
Shiota
N
N
Yamamoto
D
D
Okunishi
H
H
Miyazaki
M
M
D000595:Amino Acid Sequence; D000804:Angiotensin II / Q000096:biosynthesis*; D000818:Animals; D002610:Cheek; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D053818:Chymases; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism
D000804:Angiotensin II; D012697:Serine Endopeptidases; D053818:Chymases