Biochemical and biophysical research communications.
Publisher:
Academic Press.. San Diego, CA : Elsevier (2002)
Frequency: Weekly (except the first week of Jan. and the last week of Dec.), 2001-
Country: United States
Language: English
Start Year:1959 -
ISSN:
0006-291X (Print)
1090-2104 (Electronic)
0006-291X (Linking)
1090-2104 (Electronic)
0006-291X (Linking)
Impact Factor
3.1
2022
| NLM ID: | 0372516 |
| (DNLM): | B14760000(s) |
| (OCoLC): | 01532958 |
| Coden: | BBRCA9 |
| Classification: | W1 BI6198 |
Evidence for the existence of two isocolipases in horse pancreas. The N-terminal amino acid sequences of two forms of colipase isolated from horse pancreas have been compared. Four sequence differences were found in the first 51 amino acids. This lead us to conclude that there are two distinct colipases in the horse pancreas.
The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase. The catalytic and non-catalytic Zn atom pairs of horse liver alcohol dehydrogenase (LADH) have been replaced sequentially either by 65Zn, Co or 65Zn and Co. The Co derivatives exhibit characteristic spectra. When Co replaces the Zn atoms which exchange secondly, enzymatic activity is altered, and both imidazole and 1,10-phenanthroline (OP) significantly modify the spectrum of the catalytic Co atoms. Further, due to the removal of cobalt, the instantaneous and reversible OP inhibition of the native enzyme becomes time-dependent and irreversible. Jointly, these data identify the pair of metal at...