Fractionation and identification of pig lymph node plasma membrane glycoproteins

Barber, Brian H.; Arya, Sudha

doi:10.1016/0161-5890(82)90333-9

Cited by 9 publications

(1 citation statement)

References 34 publications

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“…The muscle-derived p3 1 molecules can be concentrated by an ion-exchange chromatography method which allows the purification of the class I1 antigens of human B lymphocytes . This method seems to be an adequate first step in the purification of the corresponding antigen heterodimers (Barber & Arya, 1982) as well as the basic p31 membrane protein in different species.…”

Section: Introductionmentioning

confidence: 99%

On a basic 31 kDa muscle membrane protein in cattle and pig, presumably equivalent to the class II antigen associated p31 molecule

Thinnes

Meyer

Schwartzenberg

1984

Animal Blood Groups and Biochemical Genetics

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In a recent paper we gave evidence by two-dimensional electrophoresis that, in man, the class I1 antigen associated glycoprotein p31 (also called Ii, In, M1, DRY, XMl)is expressed not only in the membranes of B lymphocytes but also in those of muscle, liver and brain. It can therefore be assumed that the p31 is not really associated with the human class I1 antigens but is a ubiquitous molecule.Here we demonstrate for the first time that the muscle membranes of cattle and pig contain corresponding polypeptides, with a molecular weight of about 3 1 kDa and an isoelectric point around 7.5, which comigrate in two-dimensional electrophoresis with p31 derived from the human muscle. Thus, in cattle and pig too, these proteins seem to be equivalent to the class I1 antigen associated p3 1, showing a tissue distribution wider than observed up t o now. The molecules can be concentrated by ion-exchange chromatography.

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Section: Introductionmentioning

confidence: 99%

On a basic 31 kDa muscle membrane protein in cattle and pig, presumably equivalent to the class II antigen associated p31 molecule

Thinnes

Meyer

Schwartzenberg

1984

Animal Blood Groups and Biochemical Genetics

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Dilsulfide‐linked receptors for mitogenic lectins on piglet lymphocytes

Chilson

Kelly-Chilson

1988

Eur J Immunol

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The interaction between leucoagglutinating phytohemagglutinin (L-PHA), concanavalin A (Con A), soybean agglutinin (SBA) and lentil lectin (LcH) with disulfide-linked cell surface receptors on lymphocytes from mesenteric lymph nodes of 3-day piglets (PMLN) was investigated. Surface radioiodinated PMLN lymphocytes were lysed with buffer containing Nonidet-P40. The lysates were adsorbed on lectin-agarose derivatives (or bovine serum albumin-agarose). Eluates from the lectin-agarose derivatives were analyzed by one-dimensional or two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis both under reducing and nonreducing conditions. Among the various-lectin-binding polypeptides, L-PHA recognizes a single 92-kDa disulfide-linked moiety in piglet lymphocyte lysate, comprised of polydisperse 52-kDa subunits. In addition to this apparent homodimer, SBA, Con A and LcH bind a much less prominent 82-kDa heterodimer comprised of 47-kDa and 37-kDa polypeptides; these molecules are not observed in eluates of L-PHA. Binding of the 92- and 82-kDa molecules by LcH is inhibited by methyl-alpha-D-mannoside. These results indicate that there are two lectin-binding disulfide-linked glycoproteins on lymphocytes from 3-day piglets which bind preferentially to potent mitogens. The electrophoretic properties of these molecules, under both reducing and nonreducing conditions, as well as their lectin-binding properties are very similar to those observed for antigen receptor molecules on lymphocytes from other species.

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Functional reassembly of lymphocyte lentil lectin receptor glycoproteins into lipid bilayer vesicles

Campbell

Ross

Sharom

1983

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Fractionation and identification of pig lymph node plasma membrane glycoproteins

Cited by 9 publications

References 34 publications

On a basic 31 kDa muscle membrane protein in cattle and pig, presumably equivalent to the class II antigen associated p31 molecule

On a basic 31 kDa muscle membrane protein in cattle and pig, presumably equivalent to the class II antigen associated p31 molecule

Dilsulfide‐linked receptors for mitogenic lectins on piglet lymphocytes

Functional reassembly of lymphocyte lentil lectin receptor glycoproteins into lipid bilayer vesicles

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