Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis (Record no. 66108)

MARC details
000 -LEADER
fixed length control field 00962nam a2200181Ia 4500
100 ## - MAIN ENTRY--AUTHOR NAME
Personal name Wajant H
245 #0 - TITLE STATEMENT
Title Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Name of publisher Plant science
Year of publication 1996
300 ## - PHYSICAL DESCRIPTION
Number of Pages 25-31
520 ## - SUMMARY, ETC.
Summary, etc Hydroxynitrile lyase from Hevea brasiliensis (HbHNL) was purified to apparent homogeneity. Purified HbHNL consists of non-covalently linked monomers of 30kDa. HbHNL exhibits a typical Michaelis-Menten kinetics with a Km of 115 mM and the enzyme activity is strongly inhibited by diisopropyl fluorophosphate and diethyl pyrocarbonate indicating a serine and histidine in the active site. HbHNL is serologically related to the HNL from Manohot esculenta but not to other HNLs.
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Cyanogenesis
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Enzyme purification
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Hevea brasiliensis
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Hydroxynitrile lyase
700 ## - ADDED ENTRY--PERSONAL NAME
Personal name Forster S
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type Journals
Holdings
Withdrawn status Lost status Damaged status Not for loan Home library Current library Shelving location Date acquired Serial Enumeration / chronology Koha item type
      Journals RRII Library RRII Library Physiology 17/12/2021 Volume 115, Issue 1 Journals