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Chemical modification of carboxypeptidase A crystals. Nitration of tyrosine-248

Biochemistry

Jan 13, 1976

G Muszynska, J F Riordan

PMID: 942853

Abstract

Nitration of bovine carboxypeptidase A crystals with tetranitromethane increases esterase activity, decreases peptidase activity, and modifies about one tyrosyl residue. Modification of enzyme crystals avoids the polymerization that occurs when the enzyme is nitrated in solution. Two pr...read more

Mentioned in this Paper

Carboxypeptidase A
Crystal - Body Material
Methane
Bos taurus
Cytokinesis of the Fertilized Ovum
Carboxypeptidase A Activity
Digests
Plasma Protein Binding Capacity
Bromides Measurement
Avazyme
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Chemical modification of carboxypeptidase A crystals. Nitration of tyrosine-248

Biochemistry

Jan 13, 1976

G Muszynska, J F Riordan

PMID: 942853

DOI:

Abstract

Nitration of bovine carboxypeptidase A crystals with tetranitromethane increases esterase activity, decreases peptidase activity, and modifies about one tyrosyl residue. Modification of enzyme crystals avoids the polymerization that occurs when the enzyme is nitrated in solution. Two pr...read more

Mentioned in this Paper

Carboxypeptidase A
Crystal - Body Material
Methane
Bos taurus
Cytokinesis of the Fertilized Ovum
Carboxypeptidase A Activity
Digests
Plasma Protein Binding Capacity
Bromides Measurement
Avazyme

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Paper Details
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  • References
  • Citations10
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  • Citations10
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