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

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...

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Bibliographic Details
Published in:Biochemistry (Easton) 1993-05, Vol.32 (20), p.5466-5471
Main Authors: Patel, Shilpa R, Evans, Steven, Dunne, Kevin, Knight, Graham C, Morgan, Peter J, Varley, Paul G, Craig, Stewart
Format: Article
Language:English
Subjects:
Acetates
Acetic Acid
Acetonitriles
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chemokine CCL4
Circular Dichroism
Cytokines - chemistry
Electrochemistry
Fluorescence Polarization
Fundamental and applied biological sciences. Psychology
Humans
Hydrogen-Ion Concentration
Macromolecular Substances
Macrophage Inflammatory Proteins
Miscellaneous
Molecular Weight
Monokines - chemistry
Protein Conformation
Proteins
Recombinant Proteins
Saccharomyces cerevisiae - genetics
Sequence Analysis
Solutions
Spectrometry, Fluorescence
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00071a024