Literature DB >> 6974174

Molecular weight analysis of Fc gamma-binding proteins of lymphoid leukemia, myeloid leukemia, and hairy-cell leukemia.

H Stein, J Thoenes, U Klatt, J Gerdes, V Müller, B Havsteen.   

Abstract

The molecular weights of EDTA-mercaptoethanol-soluble Fc gamma-affined proteins isolated from chronic lymphocytic leukemia of the B type, prolymphocytic leukemia of the B type, chronic myeloid leukemia and hairy-cell leukemia were compared. SDS polyacrylamide gel electrophoresis of the Fc gamma-binding material obtained from all six cases of B type leukemia revealed a single peak with an apparent molecular weight of 28,000. The Fc gamma-affined material isolated from the cells of two cases of chronic myeloid leukemia showed two peaks, one with an apparent molecular weight of 42,600 and one with an apparent molecular weight of 18,800. The Fc gamma-affined material isolated from the cells of two cases of hairy-cell leukemia electrophoresed in the form of a closely spaced double peak. One component of the double peak had an apparent molecular weight of 28,000 and thus corresponds to the Fc gamma-binding material of leukemic B cells. The second component had a slightly lower molecular weight. The latter component is not present on either leukemic B cells or myeloid cells. The results indicate that the EDTA-mercaptoethanol-soluble Fc gamma-affined proteins of different types of cells differ in molecular weight, and thus in molecular structure.

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Year:  1981        PMID: 6974174     DOI: 10.1007/BF00405067

Source DB:  PubMed          Journal:  J Cancer Res Clin Oncol        ISSN: 0171-5216            Impact factor:   4.553


  15 in total

1.  The characterization of IgG receptor induced by human cytomegalovirus.

Authors:  S Sakuma; T Furukawa; S A Plotkin
Journal:  Proc Soc Exp Biol Med       Date:  1977-06

2.  Structure of mouse Fc receptor.

Authors:  A Bourgois; E R Abney; R M Parkhouse
Journal:  Eur J Immunol       Date:  1977-10       Impact factor: 5.532

3.  Membrane proteins of the P388D1 macrophage cell line: isolation of membrane polypeptides that bind to the Fc portion of aggregated IgG.

Authors:  M D'Urso-Coward; R E Cone
Journal:  J Immunol       Date:  1978-11       Impact factor: 5.422

4.  Biochemical characterization of an Fc receptor of rabbit lymphocytes.

Authors:  J Sire; B Kahn-Perles; A Collé; A Bourgois
Journal:  Eur J Immunol       Date:  1980-02       Impact factor: 5.532

5.  Isolation of an Fcgamma-binding protein from the cell membrane of a macrophage-like cell line (P388D1) after detergent solubilization.

Authors:  S R Loube; T C McNabb; K J Dorrington
Journal:  J Immunol       Date:  1978-03       Impact factor: 5.422

6.  Isolation and characterization of a human mononuclear cell Fc receptor.

Authors:  C Cunningham-Rundles; F P Siegal; R A Good
Journal:  Immunochemistry       Date:  1978-06

7.  Affinity isolation and characterization of immunoglobulin G Fc fragment-binding glycoprotein from human blood platelets.

Authors:  C M Cheng; J Hawiger
Journal:  J Biol Chem       Date:  1979-04-10       Impact factor: 5.157

8.  Isolation and properties of a murine spleen cell Fc receptor.

Authors:  L Rask; L Klarkeskog; L Ostberg; P A Peterson
Journal:  Nature       Date:  1975-09-18       Impact factor: 49.962

9.  Isolation of a murine leukemia FC receptor by selective release induced by surface redistribution.

Authors:  S M Cooper; Y Sambray
Journal:  J Immunol       Date:  1976-08       Impact factor: 5.422

10.  Purification of Fc gamma receptor from rabbit alveolar macrophages that retains ligand-binding activity.

Authors:  A Kulczycki; V Krause; C C Killion; J P Atkinson
Journal:  J Immunol       Date:  1980-06       Impact factor: 5.422

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  1 in total

1.  Modulation of human peripheral blood lymphocyte Fc gamma receptors by immune complexes: recovery of Fc gamma receptors in the presence of normal human serum.

Authors:  F M Reid; M G Peel; F Jarrett; G P Sandilands
Journal:  Immunology       Date:  1983-02       Impact factor: 7.397

  1 in total

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