Untersuchungen über Gamma-Makroglobuline des menschlichen Serums

Schultze, H. E.; Haupt, H.; Heide, K.; Möschlin, G.; Schmidtberger, R.; Schwick, G.

doi:10.1515/znb-1962-0506

Cited by 36 publications

(9 citation statements)

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“…A relatively constant chemical composition has been described for 7Mglobulin carbohydrate (6,(9)(10)(11)(12)(13). All descriptions present in the literature would fall into our group I dass of carbohydrate.…”

Section: Discussionmentioning

confidence: 95%

CHEMICAL CHARACTERIZATION OF GLYCOPEPTIDES FROM HUMAN ΓM-Globulins

Davie

Osterland

1968

The Journal of Experimental Medicine

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The three major classes of immunoglobulins 3'G, 3'A, and ~M contain different amounts of carbohydrate. Considerable data are now available on the number and location of the carbohydrate units on the polypeptide chains of ~/Gglobulins, but as yet little information exists for 3'M. The 3,M-globulins have approximately 10% of their mass made up of carbohydrate. In spite of this large mass, neither distribution, linkage, location, nor functional importance of this moiety is known. Among the several reasons for this paucity of information is the difficulty in securing large amounts of pure 3,M-globulin, plus the problems in structural analysis of complex oligosaccharides.The present study is devoted to two aspects of the chemistry of the carbohydrate moiety of 3'M. First is a survey of the carbohydrate composition of several pathological macroglobulins to investigate its constancy of composition. This study demonstrates that macroglobulins can be divided into at least two major groups on the basis of their carbohydrate composition. Second is a study in detail of the carbohydrate portions from highly purified macroglobulins of each group with a view to defining carbohydrate units, including their size and number, as they appear on the parent molecule. Materials and MethodsPreparation of "gM-Globulin.--Serum was obtained in the course of plasmapheresis therapy of patients with WaldenstrSm's macroglobulinemia. Sera, selected for euglobulin properties, were either diluted in ten-fold their volumes of distilled water or dialyzed against 1000-fold their volumes of 0.0015 M phosphate, pH 6.0. The centrifuged euglobulin precipitate was dissolved in neutral phosphate-buffered saline, and the solution was cleared by high speed centrifugation or filtration through Millipore filters. Small molecular weight contaminants were removed by filtration through a calibrated column of Sephadex G-200 having a total

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Section: Discussionmentioning

confidence: 95%

CHEMICAL CHARACTERIZATION OF GLYCOPEPTIDES FROM HUMAN ΓM-Globulins

Davie

Osterland

1968

The Journal of Experimental Medicine

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“…Total hexosamine was assayed by the ELSON-MORGAN reaction 32 after hydrolysis in 2N HC1 at 100°C for 12 h. The cystein/sulfuric acid method 33 for the assay offucose was used with the modification of SCHULTZE et al 34 . Total hexosamine was assayed by the ELSON-MORGAN reaction 32 after hydrolysis in 2N HC1 at 100°C for 12 h. The cystein/sulfuric acid method 33 for the assay offucose was used with the modification of SCHULTZE et al 34 .…”

Section: Carbohydrate Analysismentioning

confidence: 99%

“…Static acidwas determined with BIAL'S Reagent 34 and standardized against a substance with known sialic acid content. The resu/ts were corrected against the extinction given by the amount of fucose present in the sample.…”

Section: Carbohydrate Analysismentioning

confidence: 99%

Isolation and Characterisation of γG Type Immunoglobulins from Bovine Serum and Colostrum

Kickhöfen¹,

Hammer²,

Scheel³

1968

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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1. A scheme is presented which shows the various steps of Chromatographie procedures employed to isolate the main components of yG type globulin from bovine serum in purified form by molarity gradient chromatography on DEAE-Sephadex A-50. About 40-50% of serum yG is composed of a fraction which has the same chromatographical behaviour as the main protein component of colostrum and other secretions. This protein is designated secretory yG or yGs. In addition to this component serum contains j l and y 2 globulin. 2. The four bovine globulins (yGs from serum and eofosirum,and 2 ) are characterized by sedimentation analysis, partial specific volume determinations, amino acid and carbohydrate analysis. The difference in molecular weight between yGsZusammenfassung: Isolierung und Charakterisierung von Immunoglobulinen des^G-Typs aus Rinderserum und -colostrum. l. Die verschiedenen Fraktionierungsschritte, welche nötig sind um die Hauptkomponenten des yG-Globulins aus Rinderserum in gereinigter Form mittels Gradientenchromatographie an DEAE-Sephadex A-50 zu gewinnen, werden in einem Schema wiedergegeben. Ungefähr 40-50% des Serum-yG-Globulins besteht aus einer Fraktion, die dasselbe chromatographische Verhalten besitzt wie die Hauptkomponente des Colostrums und anderer Sekrete. Dieses Protein wird Sekret-yG oder yGs genannt. Zusätzlich zu dieser Komponente enthält Serum y r und y 2 -Globulin.

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“…Based upon these reports, it is suggested that increased levels of a 2-globulin may be of prognostic value as an indicator of the clinical stage of prostatic malignancy once the diagnosis has been made. In view of the close parallel of the high incidence of patients with prostatic cancer possessing an elevated level of a2 -globulin and that of patients with nephrosis (47), selected serum specimens were further evaluated by ultracentrif ugation and radial immunodiffusion to determine if tine observed elevation in a 2-globulin might have been due (as in nephrosis) to increased levels of a 2-macroglobulin (22,34,43). No elevation of the 19S peak or of the level of a 2-macroglobulin was detected.…”

Section: Discussionmentioning

confidence: 99%

Alterations of α<sub>2</sub> -Globulin and the Clinical Response in Patients with Prostatic Cancer following Cryotherapy

Ablin¹,

Gonder²,

Soanes³

1975

Oncology

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Evaluation of alterations in the level of α₂-globulin in the serum of 18 patients with prostatic cancer prior to and following cryotherapy of their primary prostatic tumor and the clinical response of these patients disclosed: (1) a progressive increase in the level of α₂ -globulin and the incidence of patients with significantly elevated levels of α₂-globulin, i.e., > 1.30 g/l00 ml, with a progression of the stage of their malignancy; (2) a decrease in the levels of α₂ -globulin in the serum of 14 of 18 (78 %) patients following cryotherapy, and (3) a favorable clinical response in 11 of 14 (79 %) patients with prostatic cancer showing a decrease in α₂ -globulin following cryotherapy. While limited to the study of a relatively small patient population, the present results suggest a prognostic potential for α₂ -globulin, particularly as applied to stage identification in prostatic cancer. Pending confirmation by evaluation of a larger patient population, it may even provide objective criteria for monitoring the clinical response of an individual following cryotherapy of the prostate.

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Untersuchungen über Gamma-Makroglobuline des menschlichen Serums

Cited by 36 publications

References 0 publications

CHEMICAL CHARACTERIZATION OF GLYCOPEPTIDES FROM HUMAN ΓM-Globulins

CHEMICAL CHARACTERIZATION OF GLYCOPEPTIDES FROM HUMAN ΓM-Globulins

Isolation and Characterisation of γG Type Immunoglobulins from Bovine Serum and Colostrum

Alterations of α<sub>2</sub> -Globulin and the Clinical Response in Patients with Prostatic Cancer following Cryotherapy

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