Document Detail

The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex.
MedLine Citation:
PMID:  1879417     Owner:  NLM     Status:  MEDLINE    
The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex, has been determined predominantly with conventional non-automatic methods. The positions of three disulfide bridges have been determined. The sequence has about 60% identity with that of a chitinase from cucumber and 95% with the N-terminal sequence of the lysozyme/chitinase of Parthenocissus quinquefolia. The half-cystine residues in hevein and cucumber chitinase are located at identical positions. Hevamine is a basic protein from the lutoids (vacuoles) of rubber latex and may have a role in plugging the latex vessels and cessation of latex flow. The differences in cellular location, charge properties and sequence between hevamine and cucumber chitinase are similar to those between class I and class II chitinases from tobacco and other plant species.
P A Jekel; B H Hartmann; J J Beintema
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  200     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1991 Aug 
Date Detail:
Created Date:  1991-10-03     Completed Date:  1991-10-03     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  123-30     Citation Subset:  IM    
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
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MeSH Terms
Amino Acid Sequence
Chitinase / chemistry*
Disulfides / chemistry
Latex / chemistry*
Molecular Sequence Data
Molecular Structure
Muramidase / chemistry*
Peptide Fragments
Peptide Mapping
Plant Proteins
Plants / enzymology*
Reg. No./Substance:
0/Disulfides; 0/Latex; 0/Peptide Fragments; 0/Plant Proteins; EC 3.2.1.-/hevamine; EC; EC

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