Robert J. Gargiulo - Miami FL Gary A. Mitchell - Miami FL Patricia M. Hudson - Miami FL Sharon P. Pochron - Miami FL Rolf M. Huseby - Miami FL Robert E. Smith - Livermore CA
Assignee:
American Hospital Supply Corporation - Evanston IL
International Classification:
C12Q 136 C12Q 138 C12Q 156 C07G 700
US Classification:
435 13
Abstract:
Fluorogenic substrates for proteolytic enzymes having the formula: ##STR1## or acid salts thereof wherein: R. sub. 1 is hydrogen-L, hydrogen-D, benzoyl, benzenesulfonyl, glutaryl, pyroglutamyl, carbobenzoxy, D-serine, or carbobenzoxy-serine; R. sub. 2 is hydrogen, phenyl, a straight, branched or cyclic alkyl having 1 to 4 carbons, or propionic acid; R. sub. 3 is hydrogen, straight or branched or cyclic alkyl having 1 to 4 carbons, 4-aminobutane, or 3-guanidylpropane; R. sub. 4 is methyl, 4-aminobutane, or 3-guanidylpropane; R. sub. 5 is a fluorogenic moiety, severable from said compound by a proteolytic enzyme and having different fluorescent property when severed from said compound than when forming part of said compound. The enzymes, when reacting with the substrate, remove the fluorogenic group R. sub. 5 producing an increase in its fluorescence.
Richard Cornelius Driscoll - Lake Forest IL Robert James Gargiulo - Miami FL Joseph L. Giegel - Miami FL
Assignee:
American Hospital Supply Corporation - Evanston IL
International Classification:
G01N 3114
US Classification:
1951035C
Abstract:
A method for the determination of amylase, based on the cleavage of colorimetric, ultraviolet absorbing or fluorometric substances, commonly referred to as chromogenic substances as p-nitrophenol derivatives of oligosaccharides of chain length 4-10 glucose units. Oligosaccharides of this chain length are resistant to cleavage by. alpha. and/or. beta. -glucosidase and contain endo-. alpha. -1,4 linkages which are required for amylase activity. Cleavage of the. alpha. -1,4 bonds by amylase produces smaller fragments which are acted upon by. alpha. -glucosidase and/or. beta. -glucosidase to liberate a chromophore. The rate of appearance of the chromophore is proportional to amylase activity and lends itself to either rate or endpoint determinations. The qualitative or quantitative measurement of amylase concentrations in a sample is useful in medical diagnosis.
Analytical Fluorogenic Substrates For Proteolytic Enzymes
Robert J. Gargiulo - Miami FL Gary A. Mitchell - Miami FL Patricia M. Hudson - Miami FL Sharon P. Pochron - Miami FL Rolf M. Huseby - Miami FL Robert E. Smith - Livermore CA
International Classification:
C07C10352
US Classification:
2601125R
Abstract:
Fluorogenic substrates for proteolytic enzymes having the formula: ##STR1## or acid salts thereof wherein: R. sub. 1 is hydrogen-L, hydrogen-D, benzoyl, benzenesulfonyl, glutaryl, pyroglutamyl, carbobenzoxy, D-serine, or carbobenzoxy-serine; R. sub. 2 is hydrogen, phenyl, a straight, branched or cyclic alkyl having 1 to 4 carbons, or propionic acid; R. sub. 3 is hydrogen, straight or branched or cyclic alkyl having 1 to 4 carbons, 4-aminobutane, or 3-guanidylpropane; R. sub. 4 is methyl, 4-aminobutane, or 3-guanidylpropane; R. sub. 5 is a fluorogenic moiety, severable from said compound by a proteolytic enzyme and having different fluorescent property when severed from said compound than when forming part of said compound. The enzymes, when reacting with the substrate, remove the fluorogenic group R. sub. 5 producing an increase in its fluorescence.
Composition And Method For Determining Transferase And Protease Activity
Robert J. Gargiulo - Miami FL Richard C. Driscoll - Lake Forest IL
Assignee:
American Hospital Supply Corporation - Evanston IL
International Classification:
G01N 3114 G01N 3316
US Classification:
435 16
Abstract:
Transferase and protease activity in homogenates and biological solutions is fluorometrically determined at wavelengths corresponding generally to those used for fluorometric NADH-linked determinations by utilizing novel substrate compositions consisting essentially of certain fluorogenic 5-aminoisophthalic acid derivatives coupled to amino acid constituents specific to the transferases and proteases under investigation.
Raymond Harth, Marge Pricolo, Eleanor Appelbaum, Susan Parke, Veronica Solimando, Allen Winters, Andrea Potter, Carol Harm, Barbara Sherman, Kathleen Stapleton