Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cytochrome bc1 complex has been isolated from rat-liver mitochondria by two different procedures. The enzyme isolated by either procedure exhibits a specific cytochrome b and cytochrome c1 heme content of approximately 8 and 4 nmol/mg protein respectively. Both preparations contain only seven polypeptides on sodium dodecylsulfate gel electrophoresis, with the following apparent molecular weights: I, 50000; II, 46000; III, 33000; IV, 25000; V, 12500; VI, 10000; VII, 5600. The polypeptide composition is identical to that of the beef-heart enzyme isolated by cholate/ammonium sulfate fractionation. Furthermore, with the exception of subunit II (core protein 2), the apparent molecular weights of the subunits are identical in the rat-liver and beef-heart enzymes.
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PMID:Isolation of the cytochrome-bc1 complex from rat-liver mitochondria. 626 24

The bluetongue virus (BTV) core particle contains 2 major polypeptides, P3 and P7, and is surrounded by an outer capsid layer that is composed of the 2 major polypeptides, P2 and P5. Analysis of the immune precipitates from soluble 14C-labelled BTV polypeptides and hyper-immune rabbit and guinea-pig sera indicated that polypeptide P2 precipitates only with homologous BTV sera. This would indicate that P2 is the main determinant of serotype specificity. It was also found that in sheep infected with BTV the P2-precipitating antibodies in the serum correlate with the neutralizing antibody titres, whereas the appearance and subsequent decline of P7-precipitating antibodies correspond well with those of the complement fixing antibodies. This suggests that BTV group specificity, as measured by a complement fixation tests, is determined by the core protein P7. This result was supported by the observation that mouse ascitic fluid, which contains a high titre of BTV-specific complement fixing antibodies and a very low titre of neutralizing antibodies, contains almost exclusively antibodies that precipitate P7.
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PMID:Identification of the serotype-specific and group-specific antigens of bluetongue virus. 627 73

A retrovirus that causes pulmonary adenomatosis, a contagious lung tumour of sheep, contains a 25 000 mol. wt. polypeptide which cross-reacts with the major core protein (p27) of Mason-Pfizer monkey virus and mouse mammary tumour virus.
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PMID:Sheep pulmonary adenomatosis: demonstration of a protein which cross-reacts with the major core proteins of Mason-Pfizer monkey virus and mouse mammary tumour virus. 631 58

The orientation of the different subunits of complex III in the yeast inner mitochondrial membrane has been investigated by several different approaches. Immunoinhibition studies of cytochrome c reductase activity in intact mitoplasts and submitochondrial particles using IgG obtained from specific antisera against complex III, the iron-sulfur protein, core protein I, and core protein II suggested a transmembranous orientation of the complex with the antigenic sites of the iron-sulfur protein exposed on the cytoplasmic surface of the membrane. A lack of immunoinhibition was observed with the IgG against either core protein suggesting that these proteins may not be involved in catalysis. Digestion of mitoplasts with chymotrypsin indicated that the protein mass of cytochromes b and c1 protrudes from the cytoplasmic surface of the membrane; however, the hemes of cytochrome b appear to be buried within the membrane while the heme of cytochrome c1 is partially exposed on the chymotrypsin-sensitive portion of the polypeptide. By contrast, the iron-sulfur protein does not protrude from the membrane as it is completely resistant to chymotrypsin digestion. Labeling with the hydrophilic membrane-impermeant probe diazobenzenesulfonate suggests that core protein II is exposed on both sides of the membrane but protrudes into the matrix; while core protein I is within the membrane. Immunoprecipitation studies of sodium dodecyl sulfate and Triton X-100-solubilized mitochondria with subunit-specific antisera suggest that cytochromes b and c1 and core protein I are tightly associated in complex III. By contrast, the iron-sulfur protein and core protein II are loosely associated with the other subunits of the complex such that they are dissociated by low concentrations of detergent.
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PMID:Topographical orientation of complex III in the yeast mitochondrial membrane. 631 51

Pemphigus foliaceus (PF) is a human autoimmune disease in which antibodies are directed against the cell surface of epidermal cells with resultant blister formation. The histopathology of these blisters indicates that cells have detached from each other, and electron microscopy of early blisters shows diminished numbers, to complete loss, of desmosomes as well as abnormalities of the tonofilament-desmosome complex. In this study we demonstrate that autoantibodies from certain PF patients bind to a desmosomal core glycoprotein called desmoglein (DG) I. Proteins in extracts of normal human epidermis were separated by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE), then transferred to nitrocellulose or 2-aminophenylthioether paper for immunoperoxidase staining. Results of these immunoblots indicated that sera from 6 of 13 PF patients specifically and intensely stained an approximately 160,000 mol wt polypeptide, "PF antigen". Such staining was not seen with normal human sera or sera from patients with pemphigus vulgaris or bullous pemphigoid, two autoimmune blistering skin diseases that are clinically, histologically, and immunochemically distinct from PF. However, rabbit antiserum directed against DGI, that was isolated from bovine muzzle desmosomes, stained a polypeptide band which co-migrated with PF antigen. Furthermore, when proteins from extracts of normal human epidermis were electrophoresed in two dimensions (isoelectric focusing, then SDS-PAGE) before transfer to nitrocellulose for immunoperoxidase staining, PF antibodies and antibodies to DGI stained identical spots. Finally, PF sera as well as PF IgG that was affinity purified with PF antigen from normal human epidermis, both selectively bound to DGI extracted from bovine muzzle desmosomes. These studies demonstrate that the human autoantibodies from certain patients with PF, a disease of epidermal cell adhesion, are directed against a desmosomal core protein.
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PMID:Human autoantibodies against a desmosomal core protein in pemphigus foliaceus. 649 2

A ternary complex of hyaluronic acid-binding region and link protein bound to hyaluronic acid was isolated from limit clostripain digests of proteoglycan aggregates isolated from the Swarm rat chondrosarcoma. Under these conditions, the hyaluronic acid-binding region has a molecular weight of approximately equal to 65,000 (HA-BR65). N-terminal amino acids in the complex were selectively 14C-carbamylated. The resulting derivatized HA-BR65 was isolated, and tryptic peptide maps were prepared and developed on two-dimensional TLC sheets. A single, labeled peptide was obtained which gave a Mr by approximately equal to 8,000 by SDS-PAGE. Chymotrypsin digestion of the ternary complex reduced the molecular weight of HA-BR65 to a polypeptide of approximately equal to 55,000 (HA-BR55) which still retains the same N-terminal tryptic peptide. Partial digestion of proteoglycan aggregates with clostripain generated a series of larger intermediates with the hyaluronic acid-binding region. Direct SDS-PAGE analysis revealed one major intermediate with approximately equal to 109,000 (HA-BR109) as well as HA-BR65. After chondroitinase digestion, two additional prominent intermediates were observed on a SDS-PAGE gel at Mr approximately equal to 120,000 (HA-BR120) and approximately equal to 140,000 (HA-BR140). All the intermediates were recognized by a monoclonal antibody specific for the hyaluronic acid-binding region, and all of them contained the same N-terminal tryptic peptide. The results indicate that the N terminus of the core protein is at the hyaluronic acid-binding end of the proteoglycan and that the chondroitin sulfate chains are first present on the core protein in a region between 109,000 and 120,000 molecular weight away from the N terminus.
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PMID:Characteristics of the core protein of the aggregating proteoglycan from the Swarm rat chondrosarcoma. 653 Apr 6

A protein identified as P85(gag-mos) was shown to be phosphorylated when immunoprecipitates from ts110 Moloney murine sarcoma virus transformed nonproducer cells (clone 6m2) were incubated with [gamma-(32)P]ATP. The in vitro-labeled 85,000-dalton phosphoprotein comigrated on NaDodSO(4)/polyacrylamide gels with authentic phosphorylated P85(gag-mos). Immunoprecipitates obtained with antisera prepared against Rauscher murine leukemia virus core protein p30 were active in the immune complex kinase assay but anti-murine leukemia virus p10 precipitates were not. Previous studies have shown that anti-p30 but not anti-p10 antisera recognize P85(gag-mos). The 6m2 clone has been shown to express P85(gag-mos) at 33 degrees C but not at 39 degrees C. Anti-p30 immune complexes from 6m2 cells maintained at 39 degrees C failed to phosphorylate the 85,000-dalton protein. Furthermore, the in vitro phosphorylated 85,000-dalton protein gave the same pattern of V8 protease-generated cleavage products as in vivo(32)P-labeled P85(gag-mos). We conclude from these results that P85(gag-mos) is phosphorylated in anti-p30 immune complex kinase reactions. Phosphoamino acid analyses indicated that the in vitro phosphorylated P85(gag-mos) contained phosphoserine and phosphothreonine. Our findings indicate that incubation of anti-p30 immunoprecipitates at 39 degrees C drastically reduced, in a specific way, the kinase activity associated with P85(gag-mos). This result and other data suggest that the kinase is virus-encoded. Because P85(gag-mos), but not Pr65(gag) is phosphorylated in anti-p30 immunoprecipitates from MuLV-MuSV ts110 producer cells, the kinase enzyme is associated with P85(gag-mos) and not gag gene products. A second major polypeptide of the size of P58(gag) was also phosphorylated in anti-p30 immunoprecipitates from cells maintained at 33 degrees C but not at 39 degrees C. Since 6m2 cells at 39 degrees C contain P58(gag), this is also consistent with the kinase activity being associated with P85(gag-mos).
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PMID:P85gag-mos encoded by ts110 Moloney murine sarcoma virus has an associated protein kinase activity. 660 Dec 72

Two distinct CsCl-stable empty particle populations were characterized in human adenovirus type 1 infected cells. Different sensitivity to proteases and polypeptide composition indicate that empty capsids A and B are degradation products of two different assembly intermediates. Both empty particle populations react with antihexon antibodies similarly to complete virions. Thus the arrangement of exposed type-specific epitopes is suggested to be unchanged during virus assembly. Experimental evidence is presented that both antifibre and antihexon antibodies trigger structural changes of complete virions, which are initiating the specific loss of core protein V from antibody-aggregated virions.
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PMID:Polypeptides and immunoreactivity of empty adenovirus type 1 particles. 667 9

The initial steps of adenovirus capsid morphogenesis and the sequence of entry of structural and nonstructural proteins into assembly-intermediate (IM) particles were investigated by pulse-chase labeling, temperature shifts, and cycloheximide inhibition of particle formation. The experiments were performed on wild-type and two assembly-defective, temperature-sensitive mutants, H2 ts 112 and H2 ts 107. The sequence of events in the adenovirus assembly can be schematized as follows. (i) Hexons, pentons, and protein IX assembled with scaffolding proteins 100K, PVIII, and PVII, precursor to the major core protein, to form a previral particle banding at a density of 1.285 in CsCl; (ii) additional incorporation of maturation and/or stabilization proteins IIIa, 50K, 39K, 28K, and PVI led to 1.295 IM; (iii) exit of 100K, 39K, and 28K, and entry of viral DNA gave rise to 1.370 IM; (iv) dephosphorylation and/or exit of 50K and exchange with core protein V and processing of precursors to VII, VI, VIII, and DNA-terminal protein resulted in formation of infectious 1.345 virion. The polypeptide composition of the new class of assembly-intermediate particles elicited by H2 ts 107 (1.285 IM), suggested that 100K, PVIII, and also PVII might serve as scaffold components for adenovirus capsid building.
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PMID:Morphogenesis of human adenovirus type 2: sequence of entry of proteins into previral and viral particles. 674 Sep 48

Our previous work showed that treatment of chick embryo cartilage proteoglycan (PG-H) with chondroitinase-AC II and keratanase yielded a protein-rich core fraction having enzymatically modified linkage oligosaccharides. The core sample has now been analyzed by tryptic peptide mapping, in which the isolated core sample contained in a single Coomassie blue-staining band from a dried slab gel is radioiodinated and treated with trypsin, and the resultant tryptic peptides are displayed two-dimensionally on a silica gel thin layer plate. The map thus obtained exhibited 22 major peptide spots, the resolution and location of which were reproducible. In order to identify regions of the core polypeptide from which the tryptic peptides are derived, PG-H was cleaved with clostripain under conditions that yield a hyaluronic acid-binding fragment with an apparent Mr = 150,000 and chondroitin sulfate-peptide clusters of smaller molecular sizes. Although the peptide maps of the two size classes of clostripain fragments differed significantly from each other, the patterns of spots, as a whole, were extensively similar to those observed with the intact core molecule. These results have provided additional evidence that PG-H has a single, nonvariable core protein structure. In addition, the technique used here will provide a versatile method for the identification of genetic types in this increasingly complex family of matrix macromolecules.
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PMID:A mapping technique for probing the structure of proteoglycan core molecules. 680 42


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