AN INVESTIGATION OF THE DISSOCIATION AND DENATURATION OF LEGUMIN BY SALTS USING LASER-LIGHT SCATTERING AND CIRCULAR-DICHROISM SPECTROSCOPY

被引：10

作者：

CHAMBERS, SJ ^{[1
]}

CARR, HJ ^{[1
]}

LAMBERT, N ^{[1
]}

机构：

[1] INST FOOD RES, COLNEY LANE, NORWICH NR4 7UA, NORFOLK, ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1037卷 / 01期

关键词：

Circular dichroism; Laser light scattering; Legumin; Protein unfolding; Subunit dissociation;

D O I：

10.1016/0167-4838(90)90102-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The dissociation of legumin, a 12 S seed storage globulin from Pisum sativum, has been studied by laser light scattering and circular dichroism spectroscopy. Salts from the Hofmeister series, in particular sodium perchlorate, were used as dissociating agents. The Mr 360 000 hexameric protein was found to dissociate first to and trimers and further to monomers, and the number of amino acids involved in the trimer-trimer interaction estimated to be 23(±4). Native legumin appears to be more strongly bound together than some analogous seed storage globulins from other plant species such as Arachis hypogaea or Sesamum indicum and the dissociation process was accompanied by some changes in conformation. © 1990.

引用

页码：66 / 72

页数：7

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