Robert P. Carty
SUNY Downstate Medical Center
35 Papers
445 Citations
Robert P. Carty is an academic researcher from SUNY Downstate Medical Center. The author has contributed to research in topics: Bovine pancreatic ribonuclease & Ribonuclease. The author has an hindex of 13, co-authored 35 publications.
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Papers
Enzymatic Characterization of the Matrix Vesicle Alkaline Phosphatase Isolated from Bovine Fetal Epiphyseal Cartilage
TL;DR: Purified matrix vesicle alkaline phosphatase from bovine fetal epiphyseal cartilage hydrolyzes a variety of phosphate esters as well as ATP and PPi, and is inhibited irreversibly by Be2+ ion, EDTA, EGTA, ethane-l-hydroxydiphosphonate, dichloromethanediphosph onate, L-cysteine, and N-ethylmaleimide.
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Crystal structure of two covalent nucleoside derivatives of ribonuclease A.
Joseph Nachman,Maria Miller,Gary L. Gilliland,Robert P. Carty,Matthew R. Pincus,Alexander Wlodawer +5 more
TL;DR: Crystal structures of two forms of ribonuclease A with deoxynucleosides covalently bound to respectively His 12 and His 119 have been solved and possible mechanisms for the reactions of bromoacetamido nucleosides with ribonuclelease A are proposed.
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Matrix vesicle enzymes in human osteoarthritis
Thomas A. Einhorn,Stanley L. Gordon,Scott A. Siegel,Charles F. Hummel,Matthew Avitable,Robert P. Carty +5 more
TL;DR: The results suggest that OA, growth plate, and even normal articular cartilage all have the potential to undergo calcification as long as both phosphate and pyrophosphate ions can be generated at sufficiently high levels.
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Experimental identification of a theoretically predicted "left-sided" binding mode for (GlcNAc)6 in the active site of lysozyme.
TL;DR: The results suggest that the terminal saccharide residues of these substrates bind to the left side of the active site cleft, as predicted from theory.
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Enzymatic characterization of the chondrocytic alkaline phosphatase isolated from bovine fetal epiphyseal cartilage.
TL;DR: Arrhenius studies using p-nitrophenyl phosphate and AMP as substrates have accounted for the ten-fold difference in V in terms of small differences in both the enthalpies and entropies of activation which are 700 cal/mol and 2.3 cal/degree per mol, respectively.
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