title: Purification and properties of collagenase from Cytophaga sp. L43-1 strain.
abstract: A collagenolytic bacterial strain was isolated from soil and was identified as Cytophaga sp. It produced several kinds of collagenase and protease. From the supernatant of a culture, a collagenase was purified as a single protein band upon SDS-PAGE and its molecular mass was estimated to be 120 kDa. Collagen and gelatin were good substrates for this enzyme. beta-Casein was cleaved by this enzyme at several sites.
authors.affiliation: Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Sasagawa
authors.forename: Y
authors.initials: Y
authors.lastname: Kamio
authors.forename: Y
authors.initials: Y
authors.lastname: Matsubara
authors.forename: Y
authors.initials: Y
authors.lastname: Matsubara
authors.forename: K
authors.initials: K
authors.lastname: Suzuki
authors.forename: H
authors.initials: H
authors.lastname: Kojima
authors.forename: K
authors.initials: K
authors.lastname: Izaki
mesh_terms: D000595:Amino Acid Sequence; D002364:Caseins / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D017364:Collagenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003589:Cytophaga / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002364:Caseins; D009842:Oligopeptides; D005780:Gelatin; D003094:Collagen; D010450:Endopeptidases; D017364:Collagenases