Results 151 to 160 of about 63,707 (195)

Pancreatic carboxypeptidases A and B in coeliac disease

Clinica Chimica Acta, 1961
Abstract Specific methods for the estimation of pancreatic carboxypeptidases A and B in human duodenal juice have been described. No statistically significant difference was found between the carboxypeptidase A or B activity of the duodenal juice of 8 coeliac patients and that of the juice of 8 control patients.
M, MESSER, C M, ANDERSON
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Purification of Carboxypeptidase B by Zinc Chelate Chromatography

Preparative Biochemistry, 1989
A method is described to purify pancreatic carboxypeptidases B (CPB), removing contaminating endoproteinases that interfere with use of CPB for carboxy-terminal analysis or modification of proteins. The separation uses zinc chelate chromatography and is based on the property that CPB has higher affinity for immobilized zinc ions than do serine ...
G L, Hortin, B L, Gibson
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Mechanistic implications of cyanide binding to carboxypeptidase B

International Journal of Peptide and Protein Research, 1982
The putative metal coordinating ligand cyanide was used to study the effects of modifications of the metal coordination sphere on the spectral properties and catalytic activity of cobalt and zinc carboxypeptidases. The absorption spectra of Co2+‐carboxypeptidase B in the presence of cyanide pointed to a direct interaction of the ligands with the metal.
N, Zisapel, M, Sokolovsky
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Purification and some properties of camel carboxypeptidase B

Molecular and Cellular Biochemistry, 1999
A carboxypeptidase B-like enzyme was purified 116-fold with a recovery of activity of 29% from a crude extract of camel pancreas by a four-step procedure consisting of two anion exchange chromatographies in succession, gel filtration and hydrophobic interaction chromatography. The enzyme was homogeneous on SDS and non-denaturing gel electrophoresis and
A, Al-Ajlan, G S, Bailey
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2 Carboxypeptidase B

1971
Publisher Summary This chapter focuses on the physical, chemical, and enzymatic properties of carboxypeptidase B. Carboxypeptidase B occurs in the cellular secretions of the pancreas of most vertebrates in the form of an inactive zymogen. Carboxypeptidase B may be isolated from the aqueous extracts of acetone powder of autolyzed porcine pancreatic ...
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Porcine carboxypeptidase B. I. Affinity chromatography and specificity

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Abstract Porcine carboxypeptidase B (peptidyl- l -lysine hydrolase, EC 3.4.2.2), was found to possess in addition to its known specificity toward basic substrates an intrinsic activity with specificity similar to that of carboxypeptidase A (peptidyl- l -amino acid hydrolase, EC 3.4.2.1).
M, Sokolovsky, N, Zisapel
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Comparative studies on human carboxypeptidases B and N

Archives of Biochemistry and Biophysics, 1979
Abstract A series of dicarboxylic acid bi-product analogs of lysine and arginine have been tested as competitive inhibitors of human pancreatic carboxypeptidase B and human plasma carboxypeptidase N. The most effective derivative was guanidinoethylmercaptosuccinic acid with K i s of 0.5 and 1.0 × 10 −6 m for Carboxypeptidases B and N ...
T J, McKay, A W, Phelan, T H, Plummer
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Metallocarboxypeptidases: A cadmium — Carboxypeptidase B with peptidase activity

Biochemical and Biophysical Research Communications, 1973
Abstract The replacement of zinc by a series of other metal ions (Co, Cd, Mn) resulted in enzymatically active carboxypeptidases both as peptidases and esterases. The effect of the metal replacement on the kinetic parameters varies for the various substrates. Cd-CPB, previously known for its lack of peptidase activity, shows enhenced activity as long
N, Zisapel, M, Sokolovsky
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[49] Carboxypeptidases A and B

1967
Publisher Summary This chapter discusses the mechanism of carboxypeptidases used for structural studies, namely––pancreatic carboxypeptidases A and B. Carboxypeptidases are enzymes that remove amino acids one at a time from the C-termini of tripeptides, higher peptides, and proteins.
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Purification of a human urinary carboxypeptidase (kininase) distinct from carboxypeptidases A, B, or N

Analytical Biochemistry, 1984
A carboxypeptidase which cleaves basic C-terminal amino acids from peptides was purified from concentrated human urine by a three-step procedure: chromatography on Affi-Gel Blue, arginine-Sepharose affinity chromatography, and gel filtration by HPLC on a TSK-G3000SW column. Urinary carboxypeptidase was purified 406-fold with an 11% yield and a specific
R A, Skidgel, R M, Davis, E G, Erdös
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