The inhibition of bovine pancreatic carboxypeptidase a by dihydroxyacetone phosphate

R. C. Adelman; A. G. Lacko

doi:10.1016/0006-291X(68)90337-9

The inhibition of bovine pancreatic carboxypeptidase a by dihydroxyacetone phosphate

R. C. Adelman, A. G. Lacko

Research output: Contribution to journal › Article › peer-review

Abstract

In a recent study of the effects of various ligands on the rate of proteolytic digestion of rabbit muscle aldolase, it was observed that dihydroxyacetone phosphate (DHAP) acts as a powerful inhibitor of bovine pancreatic carboxypeptidase A (CPA) (Adelman et al., 1968). The present work demonstrates that this inhibition is competitive for both peptidase and esterase activities. Because this represents the first observation of competitive inhibition of CPA by a compound lacking an aromatic group, it was of interest to characterize further the structural requirements for this interaction.

Original language	English
Pages (from-to)	596-601
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	33
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(68)90337-9
State	Published - 25 Nov 1968

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title = "The inhibition of bovine pancreatic carboxypeptidase a by dihydroxyacetone phosphate",

abstract = "In a recent study of the effects of various ligands on the rate of proteolytic digestion of rabbit muscle aldolase, it was observed that dihydroxyacetone phosphate (DHAP) acts as a powerful inhibitor of bovine pancreatic carboxypeptidase A (CPA) (Adelman et al., 1968). The present work demonstrates that this inhibition is competitive for both peptidase and esterase activities. Because this represents the first observation of competitive inhibition of CPA by a compound lacking an aromatic group, it was of interest to characterize further the structural requirements for this interaction.",

author = "Adelman, {R. C.} and Lacko, {A. G.}",

note = "Funding Information: This work was supported by grants from the National Institute General Medical Sciences, National Institutes of Health (GM 11301), the National Science Foundation (GB 7140). This is Communication from the Joan and Lester Avnet Institute of Molecular Biology.",

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AU - Lacko, A. G.

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N2 - In a recent study of the effects of various ligands on the rate of proteolytic digestion of rabbit muscle aldolase, it was observed that dihydroxyacetone phosphate (DHAP) acts as a powerful inhibitor of bovine pancreatic carboxypeptidase A (CPA) (Adelman et al., 1968). The present work demonstrates that this inhibition is competitive for both peptidase and esterase activities. Because this represents the first observation of competitive inhibition of CPA by a compound lacking an aromatic group, it was of interest to characterize further the structural requirements for this interaction.

AB - In a recent study of the effects of various ligands on the rate of proteolytic digestion of rabbit muscle aldolase, it was observed that dihydroxyacetone phosphate (DHAP) acts as a powerful inhibitor of bovine pancreatic carboxypeptidase A (CPA) (Adelman et al., 1968). The present work demonstrates that this inhibition is competitive for both peptidase and esterase activities. Because this represents the first observation of competitive inhibition of CPA by a compound lacking an aromatic group, it was of interest to characterize further the structural requirements for this interaction.

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JO - Biochemical and Biophysical Research Communications

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ER -

The inhibition of bovine pancreatic carboxypeptidase a by dihydroxyacetone phosphate

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