家蚕血淋巴中两种30 kDa蛋白质的分离、纯化、结晶及初步X射线研究。
Isolation, purification, crystallization and preliminary X-ray studies of two 30 kDa proteins from silkworm haemolymph.
作者信息
Pietrzyk Agnieszka J, Bujacz Anna, Łochyńska Małgorzata, Jaskólski Mariusz, Bujacz Grzegorz
机构信息
Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):372-6. doi: 10.1107/S1744309110054564. Epub 2011 Feb 25.
Abstract
Juvenile hormone-binding protein (JHBP) and the low-molecular-mass lipoprotein PBMHP-12 belong to a group of 30 kDa proteins that comprise the major protein component of the haemolymph specific to the fifth-instar larvae stage of the mulberry silkworm Bombyx mori L. Proteins from this group are often essential for the development of the insect. In a project aimed at crystallographic characterization of B. mori JHBP (BmJHBP), it was copurified together with PBMHP-12. Eventually, the two proteins were isolated and crystallized separately. The BmJHBP crystals were orthorhombic (space group C222(1)) and the PBMHP-12 crystals were triclinic. The crystals diffracted X-rays to 2.9 Å (BmJHBP) and 1.3 Å (PBMHP-12) resolution.
摘要
保幼激素结合蛋白（JHBP）和低分子量脂蛋白PBMHP - 12属于一组30 kDa的蛋白质，它们构成了家蚕（Bombyx mori L.）五龄幼虫阶段血淋巴中的主要蛋白质成分。该组蛋白质通常对昆虫发育至关重要。在一个旨在对家蚕JHBP（BmJHBP）进行晶体学表征的项目中，它与PBMHP - 12一起被共纯化。最终，这两种蛋白质被分别分离并结晶。BmJHBP晶体为正交晶系（空间群C222(1)），PBMHP - 12晶体为三斜晶系。这些晶体将X射线衍射至2.9 Å（BmJHBP）和1.3 Å（PBMHP - 12）的分辨率。
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