A CONTINUOUS, AUTOMATIC METHOD FOR THE STUDY OF RATE OF HYDROLYSIS OF PEPTIDES AND AMIDES.
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Amides↗
Biomedical subjects
G P HESS
Publications and source records attributed to G P HESS.
CHARACTERIZATION OF A REVERSIBLY FORMED ENZYME COMPLEX IN THE REACTION OF CHYMOTRYPSIN WITH DIISOPROPYL FLUOROPHOSPHATE.
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Chemical Phenomena↗
AN APPROACH TO THE SPECIFIC CLEAVAGE OF PEPTIDE BONDS. II. SPECIFIC CLEAVAGE OF PEPTIDE CHAINS BASED ON THE HYDROGEN FLUORIDE-INDUCED NITROGEN TO OXYGEN ACYL SHIFT.
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Amino Acids↗
Interpretation of the ultraviolet spectrum of trans-cinnamoyl-alpha-chymotrypsin.
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Chymotrypsin↗
Difference spectrum of diisopropylphosphoryltrypsin versus trypsin.
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Humans↗
Conformational changes in enzyme catalysis.
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Catalysis↗
The N, O peptidyl shift in anhydrous hydrogen fluoride.
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Fluorides↗
A rapid method for the quantitative assay of proteolytic enzymes.
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Biological Assay↗
Evidence for the involvement of a tryptophan residue in the reaction of diisopropylphosphorofluoridate with alpha-chymotrypsin.
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Chymotrypsin↗
Reactivity and interrelationship of intermediates in the hydrolysis of p-nitrophenyl acetate catalysed by chymotrypsin.
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Catalysis↗
Studies of the enzymically active material in acetyltrypsin autolysates.
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Humans↗
Distribution studies on partial peptic hydrolysates of adrenocorticotropic hormone.
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Adrenocorticotropic Hormone↗
Preparation of nonprotein fractions possessing adrenocorticotropic activity from fresh sheep pituitary glands.
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Adrenocorticotropic Hormone↗
Preparation of nonprotein fractions possessing adrenocorticotropic activity from sheep ACTH protein.
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Adrenocorticotropic Hormone↗