Psychrophilic trypsin-type protease from Serratia proteamaculans.
A preparative method for purification of a novel protease from the psychrotolerant Gram-negative microorganism Serratia proteamaculans (PSP) was developed using affinity chromatography on BPTI-Sepharose. It yielded electrophoretically homogeneous PSP preparation of 60 kD. The PSP properties (temperature and pH stability, high catalytic efficiency) indicate that this enzyme can be defined as a psychrophilic protease. Inhibitory analysis together with substrate specificity indicates that the studied PSP exhibits properties of serine trypsin-like and Zn-dependent protease.
Mikhailova
A G
AG
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. anna@enzyme.siobc.ras.ru
Likhareva
V V
VV
Khairullin
R F
RF
Lubenets
N L
NL
Rumsh
L D
LD
Demidyuk
I V
IV
Kostrov
S V
SV
D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004795:Enzyme Stability / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D012705:Serratia / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature; D014357:Trypsin / Q000378:metabolism*
D001426:Bacterial Proteins; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D014357:Trypsin