Jekel P A, Hartmann B H, Beintema J J
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
Eur J Biochem. 1991 Aug 15;200(1):123-30. doi: 10.1111/j.1432-1033.1991.tb21057.x.
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.
橡胶树胶乳中具有溶菌酶/几丁质酶活性的酶——橡胶树几丁质酶（hevamine）的一级结构主要是通过传统的非自动方法确定的。已确定了三个二硫键的位置。该序列与黄瓜几丁质酶的序列约有60%的同一性，与五叶地锦溶菌酶/几丁质酶的N端序列有95%的同一性。橡胶素（hevein）和黄瓜几丁质酶中的半胱氨酸残基位于相同位置。橡胶树几丁质酶是一种来自橡胶胶乳液泡（ lutoids）的碱性蛋白质，可能在堵塞胶乳管和停止胶乳流动中起作用。橡胶树几丁质酶与黄瓜几丁质酶在细胞定位、电荷性质和序列上的差异类似于烟草和其他植物物种中I类和II类几丁质酶之间的差异。
