Characterization of the quaternary structure and conformational properties of the human stem cell inhibitor protein LD78 in solution.

Abstract:

:The human LD78 protein (sometimes referred to as human macrophage inflammatory protein-1 alpha) has been shown to protect multipotential hemopoietic stem cells from the effects of cytotoxic agents. Administration of the recombinant stem cell inhibitor molecule LD78 as an adjunct to chemotherapy has potential clinical benefit in reducing or preventing the neutropenia associated with this treatment. At physiological ionic strength, the 8-kDa LD78 molecule exists as soluble, heterogeneous, multimeric complexes of mass ranging from 100 to > 250 kDa. The hydrodynamic and structural properties of LD78 have been determined in various buffer solutions using analytical ultracentrifugation, circular dichroism, and fluorescence spectroscopy. The results demonstrate that defined, homogeneous monomer and tetramer forms of LD78 can be prepared which display distinct conformational properties. The combined use of hydrodynamic and spectroscopic analysis provides an insight into the pathway and molecular mechanics of LD78 self-association.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Patel SR,Evans S,Dunne K,Knight GC,Morgan PJ,Varley PG,Craig S

doi

10.1021/bi00071a024

subject

Has Abstract

pub_date

1993-05-25 00:00:00

pages

5466-71

issue

20

eissn

0006-2960

issn

1520-4995

journal_volume

32

pub_type

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