Isolation and characterization of a novel acid proteinase, tropiase, from Candida tropicalis IFO 0589.
A novel acid proteinase (Tropiase) was isolated from Candida tropicalis IFO 0589 by DE52-cellulose, and DEAE-Cosmogel column chromatographies. The purified tropiase gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The enzyme preparation had a molecular weight of 23,900, isoelectric point of pH 5.1, optimum pH range of 7 to 9 and possessed 208 amino acid residues. The enzyme hydrolyzed casein, fibrinogen, keratin and collagen. The purified tropiase demonstrated hemorrhagic and capillary permeability-increasing activities. Inhibition of tropiase occurred with leupeptin and N-bromosuccinimide, however, no inhibition was observed with alpha(2)-macroglobulin, soybean trypsin inhibitor, benzamidine-HCl or diisopropyl fluorophosphate.
Okumura
Yoshiyuki
Y
Department of Quality Control, Mathuurayakugyo Co., Ltd., Aichi, Japan.
Inoue
Naomasa
N
Nikai
Toshiaki
T
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000502:physiology; D001974:Bromosuccinimide / Q000494:pharmacology; D041022:Candida tropicalis / Q000201:enzymology* / Q000472:pathogenicity; D002364:Caseins; D002845:Chromatography; D004586:Electrophoresis; D005340:Fibrinogen; D006168:Guinea Pigs; D006868:Hydrolysis; D007526:Isoelectric Point; D007976:Leupeptins / Q000494:pharmacology; D008970:Molecular Weight
D002364:Caseins; D007976:Leupeptins; D005340:Fibrinogen; D016282:Aspartic Acid Endopeptidases; C032854:leupeptin; D001974:Bromosuccinimide