| Identification | Back Directory | [Name]
CARBOXYPEPTIDASE B | [CAS]
9025-24-5 | [Synonyms]
PROTAMINASE
EC 3.4.17.2
IUB: 3.4.17.2
CARBOXYPEPTIDASE B
PROTEIN CARBOXYPEPTIDASE B
Protaminase, AEBSF treated
CARBOXYPEPTIDASE B-DFP TYPE I
RecoMbinant Carboxypeptidase B
carboxypeptidase B from hog pancreas
CARBOXYPEPTIDASE B, PORCINE PANCREAS
PEPTIDYL-L-LYSINE[L-ARGININE] HYDROLASE
CARBOXYPEPTIDASE B, AEBSF TREATED, FROM
carboxypeptidase b from porcine pancreas
sequencing recombinant carboxypeptidase B
Carboxypeptidase B, AEBSF treated hog pancreas
carboxypeptidase B from procine*pancreas protease
CARBOXYPEPTIDASE B FROM PROCINEPANCREAS PROTEASE I
Carboxypeptidase B froM porcine pancreas(PMSF Treated)
Peptidyl-L-lysine(L-arginine) hydrolase, Protaminase
Carboxypeptidase B, AEBSF treated from hog pancreas | [EINECS(EC#)]
232-788-9 | [Molecular Formula]
C31H38N4O7S | [MDL Number]
MFCD00081476 | [MOL File]
9025-24-5.mol | [Molecular Weight]
610.721 |
| Chemical Properties | Back Directory | [storage temp. ]
−20°C
| [form ]
powder
| [color ]
white
| [biological source]
Porcine pancreas | [Water Solubility ]
water: 1mg/mL | [Specific Activity]
50-55units/mg protein carboxypeptidase B |
| Hazard Information | Back Directory | [Uses]
Carboxypeptidase B from Sigma has been used as a reference for assaying carboxypeptidase activity in lysed pituitary granules derived from the anterior and intermediate lobes of rat. The enzyme has also been used to digest plasma samples by removing C-terminal basic amino acids, to get a distinct band for each allotype during C4 electrophoresis. | [Uses]
The enzyme from Sigma has been used to develop homogeneous time-resolved fluorescence (HTRF) assay for measuring carboxypeptidase B activity in a miniaturized high-throughput screening format. It has been used to evaluate the impact of the C-terminal lysine(s) in human plasminogen binding to Bifidobacterium. The effect of treatment with carboxypeptidase B, which is a C-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis. | [General Description]
Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators. | [Biochem/physiol Actions]
Carboxypeptidase B is a proteolytic enzyme capable of rapidly hydrolyzing peptide bonds to release certain carboxyl-terminal basic amino acids from peptides and proteins. Its molecular mass is 34,300±600 Da. It contains one non-dialyzable gram atom of zinc per mole. The enzyme activity is inhibited by metal chelating agents 1, 10-phenanthroline, 8-hydroxyquinoline-5-sulfonic acid, and 2,2′-dipyridyl. |
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