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Chemical kinetics / Metabolism / Biomolecules / Enzyme / Chitinase / Peptidoglycan glycosyltransferase / Chemistry / Catalysis / Physical chemistry


ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS Vol. 344, No. 2, August 15, pp. 335–342, 1997 Article No. BB970225 Kinetic Analysis of Barley Chitinase1
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Document Date: 2005-01-04 12:23:46

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City

Banerjee / Pinsdorf / HOLLIS ET / New York / Wiley / /

Company

Amicon Co. / Steady-State Enzyme Systems / ACE / SLM / Tosoh / Honda / /

Currency

USD / /

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Facility

Plant J. / Plant Physiol / University of Texas / Plant Mol. / /

IndustryTerm

active site / aglycone product / methylumbelliferone / substrate solutions / hydrolysis products / authentic saccharide solution / free energy / purified chitinase solution / catalytic site / cleavage products / chitinase solution / reaction products / substrate solution / resultant solution / free energy differences / energy calculations / /

Organization

Foundation for Research / Department of Food and Nutrition / Department of Chemistry and Biochemistry / Welch Foundation / University of Texas / /

Person

Thomas Hollis / Yuji Honda / † Tamo / Mundy / Genet / Prasad / V / Lawrence Poulsen / Philip J. Day / Microbiol / Jon D. Robertus / Turk / V / Edward Marcotte / Klaus Linse / Kd / Sharon / Austin Texas / /

Position

King / kinetic model / General / inappropriate model for chitinase / /

Product

Barley Chitinase1 Thomas / sodium acetate / /

ProvinceOrState

Alabama / S. K. / Florida / New York / /

Technology

electrophoresis / X-ray / carried out using capillary electrophoresis / /

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