The purification and characterization of a proline dipeptidase from guinea pig brain.
نویسندگان
چکیده
منابع مشابه
Isolation, Purification and Characterization of Proline Dehydrogenase from a Pseudomonas putida POS-F84 Isolate
The purpose of this study was to isolate and characterize Proline Dehydrogenase (ProDH) enzyme frommicroorganisms isolated from soil in Iran. Isolation and screening of L-proline degradative enzymes from soilsamples was carried out. The isolate was characterized by biochemical markers and 16S rRNA geneanalysis. The target ProDH was purified and the effects of pH and temperatur...
متن کاملPurification and Characterization of a Dipeptidase from Streptococcus cremoris Wg2.
A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 49,000. The dipeptidase is capable of hydrolyzing a range of dipeptides, ...
متن کاملVesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase.
A large number of chemokines, cytokines, and signal peptides share a highly conserved X-Pro motif on the N-terminus. The cleavage of this N-terminal X-Pro dipeptide results in functional alterations of chemokines such as RANTES, stroma-derived factor-1, and macrophage-derived chemokine. Until recently, CD26/DPPIV was the only known protease with the ability to cleave N-terminal X-Pro motifs at ...
متن کاملPurification and characterization of guanosine 3':5'-monophosphate-specific phosphodiesterase from guinea pig lung.
A low K,,, guanosine 3’:5’-monophosphate (cyclic GMP)specific phosphodiesterase was purified about 250-fold from crude extracts of the guinea pig lung by steps of DEAEcellulose chromatography, hydroxylapatite treatment, and preparatory polyacrylamide gel electrophoresis. Analytical gel electrophoresis revealed two protein bands, indicating that the enzyme preparation was about 50% homogeneous. ...
متن کاملPurification and Characterization of Guanosine 3’S’- Monophosphate-specific Phosphodiesterase from Guinea Pig Lung*
A low K,,, guanosine 3’:5’-monophosphate (cyclic GMP)specific phosphodiesterase was purified about 250-fold from crude extracts of the guinea pig lung by steps of DEAEcellulose chromatography, hydroxylapatite treatment, and preparatory polyacrylamide gel electrophoresis. Analytical gel electrophoresis revealed two protein bands, indicating that the enzyme preparation was about 50% homogeneous. ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)32385-8