Physical, Chemical, and Immunological Studies on Globulins From Multiple Myeloma

Smith, Emil L.; Brown, Douglas M.; McFadden, Mary L.; Buettner-Janusch, Vina; Jäger, B

doi:10.1016/s0021-9258(19)81417-5

Cited by 54 publications

(5 citation statements)

References 47 publications

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“…All of the fl-myeloma proteins encountered in this study were found to contain considerably more hexose, hexosamine, and sialic acid than the ~,-myeloma type or normal "g-globulin. Smith and associates (10) in a detailed study of the amino acid composition of four myeloma proteins also noted that one, with more rapid mobility, contained more carbohydrate than the others.…”

Section: Electrophoresismentioning

confidence: 94%

“…The high carbohydrate content, particularly of the portion that appears to be sialic acid, may contribute to the more acid characteristics of the more rapidly migrating fl-type proteins discussed above. The difference in carbohydrate may also account for some of the immunological differences between the 3,-and fl-type proteins (8,10).…”

Section: Electrophoresismentioning

confidence: 99%

“…A certain amount of evidence has accumulated (34,10) in support of the idea that the myeloma proteins represent huge elevations of individual components of the normal spectrum of ~/-globulins. There remain a few observations, however, that are difficult to explain in terms of this concept.…”

Section: Electrophoresismentioning

confidence: 99%

“…The purpose of the present study was to investigate quantitatively the carbohydrate content of various components of serum "r-globulin as well as the pathological myeloma proteins which are immunologicaUy related to these normal proteins (8)(9)(10). Five preparations of ~/-globulin and twelve myeloma proteins were isolated electrophoretically and analyzed for hexose, fucose, hexosamine, and sialic acid.…”

mentioning

confidence: 99%

“…Various myeloma proteins have been found to differ markedly in electrophoretic mobility (17) and in their immunological specificity (8,18,19). The possible role of the carbohydrate constituents of these proteins in accounting for their differences has not been ascertained, although some evidence on this point has recently been reported by Smith and associates (10) and from this laboratory (20). Determination 253…”

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confidence: 99%

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The CARBOHYDRATE OF Γ-Globulin AND MYELOMA PROTEINS

Müller‐Eberhard

Kunkel

1956

The Journal of Experimental Medicine

146

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Fractions of serum consisting primarily of 7-globulin as determined by electrophoresis have been shown to contain protein-bound carbohydrate (1-3). However, recent evidence concerning the electrophoretic inhomogeneity of ~/-globulin (4-6) as well as the finding of secondary components in the ultracentrifuge (7) which might be high in carbohydrate has caused uncertainty regarding the existence of carbohydrate as a distinct constituent of the various species of proteins making up this fraction of serum.The purpose of the present study was to investigate quantitatively the carbohydrate content of various components of serum "r-globulin as well as the pathological myeloma proteins which are immunologicaUy related to these normal proteins (8-10). Five preparations of ~/-globulin and twelve myeloma proteins were isolated electrophoretically and analyzed for hexose, fucose, hexosamine, and sialic acid. A method of zone electrophoresis was developed employing a polyvinyl chloride supporting medium which was particularly suited for carbohydrate analyses of separated fractions. It was found that various *t-globulin preparations from normal and pathological sera which were homogeneous in the ultracentrifuge contain a similar amount of carbohydrate. This was also true of certain of the myeloma proteins of the ~/-globulin type. The fl-myeloma proteins showed a higher carbohydrate content.Gamma globulin separated from normal serum using filter paper electrophoresis has been variously reported to be periodic acid-Schiff (PAS) negative (11, 12) and positive (13,14). Myeloma proteins have been stained with PAS after paper electrophoresis and were found to exhibit an intense PAS reaction (11,15,16). This finding has been interpreted to indicate that the myeloma proteins represent abnormal glycoproteins. These studies, however, were not quantitative and the protein-carbohydrate ratio could not be determined for comparison with normal ~/-globulin. Various myeloma proteins have been found to differ markedly in electrophoretic mobility (17) and in their immunological specificity (8,18,19). The possible role of the carbohydrate constituents of these proteins in accounting for their differences has not been ascertained, although some evidence on this point has recently been reported by Smith and associates (10) and from this laboratory (20). Determination

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Section: Electrophoresismentioning

confidence: 94%

Section: Electrophoresismentioning

confidence: 99%

Section: Electrophoresismentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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