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Characterization of a Human Macroglobulin

IV. STUDIES OF ITS CONFORMATION BY FLUORESCENCE POLARIZATION

From the ¹ From the Arthritis and Rheumatism Branch and the Clinical Endocrinology Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

The mean rotational relaxation times of human macroglobulin (M) conjugated with 1-dimethylaminonaphthalene-5-sulfonyl-chloride, its subunit (M_s), and its tryptic fragment (Fabµ) have been determined by the technique of polarization of fluorescence. Strikingly low values were found for M (80 nsec) and M_s (69 nsec). These low values as well as other properties of M and M_s are consistent with internal degrees of rotational freedom. The Fabµ fragment had a relaxation time indicative of a compact structure, and it is suggested that it may represent the effective rotational subunit in M.

Parallel studies with human 7 S ₂-globulin (G) immunoglobulin and with its papain fragments yielded results and conclusions similar to those determined for M and to those reported for G of other species.

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