The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex.
Eur J Biochem
; 200(1): 123-30, 1991 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-1879417
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Plantas
/
Muramidase
/
Quitinases
/
Látex
País/Região como assunto:
America do sul
/
Brasil
Idioma:
En
Revista:
Eur J Biochem
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Holanda