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56 Carbodiimide modification of proteins

Published in: Methods in Enzymology

Date of publication: January 1, 1972

Language: English

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Cites articles 16

Date

Title

Authors

March 1, 1963

Direct evidence for the presence of histidine in the active center of chymotrypsin,Direct Evidence for the Presence of Histidine in the Active Center of Chymotrypsin*
June 1, 1964

ANTIBODIES TO BRADYKININ AND ANGIOTENSIN: A USE OF CARBODIIMIDES IN IMMUNOLOGY
December 1, 1965

The chemistry and use of cellulose derivatives for the study of biological systems
January 1, 1966

Structural studies of ribonuclease. XXI. The reaction between ribonuclease and a water-soluble carbodiimide
September 1, 1967

A method for modification of carboxyl groups in proteins: its application to the association of bovine beta-lactoglobulin A,A method for modification of carboxyl groups in proteins: Its application to the association of bovine β-lactoglobulin A
January 1, 1967

Modification of the carboxyl groups of ribonuclease by attachment of glycine or alanylglycine,Modification of the Carboxyl Groups of Ribonuclease by Attachment of Glycine or Alanylglycine*
June 1, 1968

Reaction of tyrosine residues in proteins with carbodiimide reagents
March 1, 1968

The reaction of hydroxamic acids with water-soluble carbodiimides. A Lossen rearrangement
May 1, 1969

Carboxyl group modification in chymotrypsin and chymotrypsinogen
August 1, 1969

The reactivity of carboxyl groups in chymotrypsinogen
October 1, 1969

The promotion of activation of bovine trypsinogen by specific modification of aspartyl residues
December 1, 1969

The glutamyl linkages in collagen
July 1, 1969

On the molecular characterization of the sodium-potassium transport adenosine triphosphatase
March 1, 1970

Reaction of carbodiimides with protein sulfhydryl groups
January 1, 1970

Modification of carboxyl groups in the active site of trypsin
February 1, 1970

Lactose synthetase. Modification of carboxyl groups in alpha-lactalbumin,Lactose synthetase modification of carboxyl groups in α-lactalbumin

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