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Myosin extracts from central white fibers and peripheral red fibers of the lateral muscle of eel (Anguilla anguilla) were analysed by electrophoresis under non-dissociating conditions, which demonstrated a polymorphism of myosin isoforms. The light and heavy subunit content of the isomyosins was established using SDS-PAGE and two-dimensional electrophoresis. In the central white muscle, 3 myosin isoforms FM3, FM2, FM1, were characterized by 3 types of fast light chain and one fast heavy chain HCf; the existence of a fourth isomyosin is discussed. In the peripheral red muscle, two myosin isoforms were found, SM1 and SM2, each characterized by a specific heavy chain, HCs1 or HCs2, and containing the same slow light chain content. This work demonstrates for the first time the existence of 3 heavy chains in the skeletal muscle of a fish.
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PMID:Myosin structure in the eel (Anguilla anguilla L.). Demonstration of three heavy chains in adult lateral muscle. 226 55

1. White skeletal muscle myosin of four marine teleost fish species (cod, blue whiting, Norway haddock, and spotted wolf-fish) was analyzed by native, SDS-PAGE, and 2-dimensional electrophoresis. 2. Four types of native myosin were present in cod, blue whiting and Norway haddock. The second fastest migrating form was predominant. 3. Myosin from spotted wolf-fish also resolved into four forms. The fastest migrating form was hardly noticeable. The other three were present in apparently similar amounts. 4. In the myosin from each species there were three types of light chains. The pattern of light chains was species specific. 5. Apparently, there was only one type of heavy chain in myosin from cod, Norway haddock and spotted wolf-fish. One preparation of cod showed an extra band of higher electrophoretic mobility than the main band. In blue whiting we found two bands present in approximately equal amounts.
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PMID:Electrophoretic study of myosin isoforms in white muscles of some teleost fishes. 236 58

The myosin contained in white and red muscles of herring (Clupea harengus harengus) was purified, and its subunit composition analyzed by electrophoretic techniques. The only myosin isoform present in red muscles was made up of one type of heavy chain and two types of light chain. The native myosin from white muscles migrated as one wide band. Analysis of the extracts by SDS/glycerol/PAGE from white muscles revealed one main type of heavy chain. Light chains were identified by SDS-PAGE analysis of electrophoretically purified myosin, and two-dimensional electrophoresis of the extracts demonstrated differences in the light chain composition of white and red muscles. Using this methodology, light chain polymorphism was detected in white muscles among members of the same species.
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PMID:Intraspecific myosin light chain polymorphism in the white muscle of herring (Clupea harengus harengus, L.). 236 52

Axolotl specific antibodies to 2,4-dinitrophenyl (DNP) were purified by affinity chromatography from the sera of animals immunized with 2,4,6-trinitrophenylated sheep red blood cells (TNP-SRBC). The purified anti-TNP/DNP antibodies, when analyzed by SDS-PAGE, were constituted of high molecular weight molecules, which in reducing conditions, were separated into heavy 72-88 kD and light 27-30 kD polypeptides. The axolotl heavy antibody chains strongly bound Concanavalin-A and migrate faster in SDS-PAGE after endoglycosidase-F (Endo-F) treatment. Using the same techniques, no carbohydrate components were detected onto light chains. Monoclonal antibodies (MAbs) were obtained against these purified axolotl immunoglobulins (Ig) and their specificities were studied by immunoblotting. MAbs 33.45.1 and 33.101.2 respectively recognized heavy and light chains determinants of the Ig molecule. These determinants were resistant to Endo-F digestion, suggesting that the two MAbs were not directed to polypeptide-associated N-linked high mannose or complex oligosaccharides. MAbs 33.45.1 and 33.101.2 were compared to 11.5.2, an anti-axolotl thymocytes MAb which was reactive for both axolotl leucocytes and soluble Ig. MAb 11.5.2 reacted in immunoblotting against several high molecular weight axolotl serum proteins, including heavy Ig chains. Light chains were not recognized. However, 11.5.2 did not further recognize Endo-F treated Ig, suggesting its specificity for a carbohydrate determinant of the heavy chain, and link to a large diversity of soluble or membrane glycoproteins.
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PMID:Characterization of axolotl heavy and light immunoglobulin chains by monoclonal antibodies. 244 89

A panel of monoclonal antibodies (mAb) was developed by the fusion of Sp2/0 myeloma cells and spleen cells from mice immunized with peripheral blood mononuclear cells (PMNC) or T cells from NIH swine leucocyte antigen (SLA) inbred miniature swine. Twenty stable hybridoma clones were isolated that secreted mAb that reacted with swine PMNC, as determined by an enzyme-linked immunosorbent assay (ELISA). The binding profile to swine PMNC and the ability to fix complement of these mAb were investigated by flow cytometric analyses. The molecular weights of the antigens recognized by six of the mAb were determined by immunoprecipitation of 125I surface-labelled PMNC, followed by SDS-PAGE under reducing conditions. The most interesting mAb, 7-34-1 (IgG2a), precipitated a putative MHC class I molecule composed of a 50,000 MW heavy chain and a 12,000 MW light chain (beta 2m). This is the third SLA class I-reactive monoclonal antibody to be described for swine. Properties of the mAb described in this paper, mAb 7-34-1, are different from the two other SLA class I-specific mAb that have been described elsewhere in the literature (mAb 74-11-10 and mAb PT85). Monoclonal antibody 7-34-1 recognized class I antigens of SLA haplotypes a, c and d in an equivalent manner. This mAb should be especially useful as a general anti-SLA class I reagent for experiments on NIH miniature swine.
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PMID:Preparation and characterization of murine monoclonal antibodies to swine lymphocyte antigens. 245 49

A number of horse alloantisera were characterized biochemically as being directed against MHC class I or class II antigens by immunoprecipitation of the corresponding antigens from lysates of biosynthetically radioactively labelled lymphocytes and determination of their molecular weights by SDS-PAGE and fluorography. Sera recognizing A2 and A3 specificities precipitated antigens of 44,000 Daltons molecular weight (class I heavy chain), whereas sera with specificities W13, W22 and W23 precipitated antigens corresponding to class II dimers (30,000 and 32,000 Daltons). Comparison with antigens precipitated from horse lymphocyte lysates using (cross-reacting) antibodies to human class I and class II MHC molecules confirmed the results obtained.
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PMID:Biochemical evidence that equine leucocyte antigens W13, W22 and W23 are present on horse major histocompatibility complex class II molecules. 251 77

The aim of the presented work was to find out whether the Fc gamma receptor from human placental syncytiotrophoblast plasma membranes in its native membrane-bound state is composed of more subunit chains than previously found in our laboratory in the purified receptor. The chains might be lost during the purification procedure with the use of various chaotropic reagents, e.g. acidic or alkaline buffers, detergents. To study this problem, affinity labeling technique and bifunctional crosslinking reagents were used to covalently link IgG with the Fc gamma receptor. The reagents used were: noncleavable dimethylsuberimidate (DMS), cleavable dimethyl 3,3-dithiobispropionimidate (DTBP), and photoactivable sulfosuccinimidyl 6-/4' azido-2'nitrophenylamino/hexanoate (sulfo-SANPAH). Human 125I-IgG were crosslinked to the membrane-bound receptor or unlabeled IgG was crosslinked to 3H-labeled placental membranes. When 125I-IgG were used in the presence of an excess of unlabeled IgG, recovery of radioactivity after crosslinking was much lower, indicating that human IgG and the placental Fc gamma receptor were involved in the formation of crosslinking of ligand-receptor complexes. The products of crosslinking were analyzed in SDS-PAGE. In the absence of reducing agents, high molecular weight products were present which did not enter the gel or formed broad diffused bands at the top of the gel. Therefore, the products of crosslinking were analyzed under reducing conditions. Analysis by SDS-PAGE demonstrated a major polypeptide band Mr of 160,000 in soluble products of crosslinking of IgG to the placental Fc gamma receptor, regardless of which noncleavable crosslinker was used. The protein is built either of two molecules of the receptor subunit chain, Mr of 60,000 and one IgG heavy chain (Mr of 56,000) or of two IgG heavy chains and one molecule of the receptor chain. The presence of this protein in control samples was not observed at all or its content was markedly lower. The same effect was also observed when DTBP, a cleavable crosslinking reagent was used. In this case, 125I-IgG heavy and light chains or the receptor subunit chains were found after SDS-PAGE under reducing conditions. The results presented in this paper do not suggest a presence of additional chains in the placental Fc gamma receptor others than described in our previous paper concerning the subunit structure of this receptor.
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PMID:Human placental Fc gamma receptor. Studies on affinity labeling of the receptor with IgG. 251 11

Protein C (PC) is a vitamin K-dependent protein which functions as both an anticoagulant and profibrinolytic. It is synthesized as a single chain protein (SC-PC) and post-translationally modified into a two chain form (2C-PC). Two chain PC consists of a light chain (LC) and a heavy chain (HC). The present study was undertaken to determine the composition of the molecular forms of PC in plasma. PC was immunoprecipitated, subjected to SDS-PAGE and Western blotting. The blots were scanned by densitometry to determine the distribution of the various forms. The percentage of SC-PC and 2C-PC was found to be 10% and 90% respectively. This is in agreement with previous work. SC-PC and the heavy chain of 2C-PC consisted of three molecular forms ("alpha", "beta", and "gamma"). The "alpha" form of HC is the standard 2C form with a MW of 40 Kd. The "beta" form of HC has also been described and has MW which is 4 Kd less than the "alpha" form. The "gamma" species of the SC and 2C-PC has not been previously described. However, its 3 Kd difference from the "beta" form could be due to modification of the "beta" species or to a separate modification of the alpha-HC. The LC of PC was shown to exist in two forms (termed form 1 and form 2). The difference between these two forms is unknown. The molecular forms of PC are most likely due to a post-translational modification (either loss of a carbohydrate or a peptide) rather than from plasma derived degradation.
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PMID:Molecular forms of human protein C: comparison and distribution in human adult plasma. 259 63

Membranes were isolated from B cells stimulated with phorbol 12-myristate 13-acetate (PMA) for a time sufficient to allow maximal redistribution and activation of protein kinase C (PKC). Exposure of such membranes to a short incubation with [gamma-32P]ATP resulted in the detection of at least nine unique or hyperphosphorylated membrane proteins by SDS-PAGE and autoradiography. The appearance of these phosphoproteins was blocked by pretreatment of the membranes with H-7 or sangivamycin, two selective inhibitors of PKC. In addition, membranes purified from B cells treated with an inactive phorbol ester or stimulated with dibutyryl cAMP failed to exhibit a pattern of new phosphoproteins. These results are consistent with the involvement of PKC in the phosphorylation of the proteins. These phosphoproteins are also candidates for proteins whose functions are modified as a consequence of early signal delivery to resting B cells following membrane immunoglobulin occupancy. This system was utilized to identify the heavy chain of MHC class I molecules as one of the membrane proteins phosphorylated by PKC. The MHC class II molecules were not phosphorylated in membranes isolated from PMA-treated normal B cells or from PMA-treated B cells which had previously been exposed to IL-4. These results indicate that class I, but not class II, MHC molecules are phosphorylated by PKC. It is possible that such a modification of cell surface class I molecules may be involved during the process of signal transduction leading to B cell activation.
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PMID:Phosphorylation of class I but not class II MHC molecules by membrane-localized protein kinase C. 263 45

Fc gamma Receptor contained in a mixture of plasma-membrane components released from pig peripheral blood lymphocytes following a 4----37 degrees C temperature shift was isolated by affinity chromatography on immobilized pig IgG. The main component of the receptor preparation exhibited an apparent molecular weight of 40-43 kDa in SDS polyacrylamide gel electrophoresis. Specificity of interaction of isolated Fc gamma receptor with immobilized pig IgG (Ka = 5.4 x 10(6) M-1) was investigated by competitive radioimmunoassay employing labelled Fc gamma receptor. The interaction was specifically inhibited by pig IgG, its Fc fragment, and less so by its pFc' fragment. Inhibition by peptides prepared from the pig IgG CH3 domain pointed to the heavy chain segment between residues 340 and 380 as the probable location of the binding site. In the competitive assay, bovine, human, mouse and guinea pig IgGs were as effective inhibitors as the homologous IgG, while rabbit IgG produced weaker inhibition. The amino acid composition of the pig lymphocyte Fc gamma receptor was determined. Comparison with the amino acid compositions of some other Fc receptors and other proteins revealed its structural relatedness to several Fc gamma receptors of lymphoid cells and to the poly-Ig receptor. In addition, the comparison of amino acid compositions suggested a structural relationship between the pig Fc gamma receptor and some seemingly unrelated proteins.
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PMID:Isolation and characterization of pig lymphocyte Fc receptor. 263 32


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