Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A macromolecular aggregate of corticotropin-beta-lipotropin common precursor had been observed in ovine pituitary preparations as an excluded fraction of Sephadex G-200 gel filtration. This fraction could not penetrate a 10% gel during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, when 2-mercaptoethanol or other disulfide-cleaving agents were not present in the buffer used to solubilize the protein preparation prior to the electrophoresis. On a 4.6% gel (acrylamide:bisacrylamide, 20:1), the material migrated as a diffuse band to a position between those of beta-galactosidase (Mr 130 000) and myosin (Mr 200 000). Both observations were consistent with an apparent Mr greatly in excess of that of the corticotropin-beta-lipotropin common precursor reported by many investigators. Neither 5% SDS nor 1% Triton X-100 could dissociate the macromolecular aggregate, but 2-mercaptoethanol and urea, either alone or in combination, were able to dissociate it to two main protein components, one of which was identified as corticotropin-beta-lipotropin with an apparent Mr of 34 000. The fact that urea alone could dissociate this macromolecular aggregate led us to believe that it might be a non-covalent aggregate and that 2-mercaptoethanol probably did not achieve the dissociation through the cleavage of an interchain disulfide bond but by bringing about conformational changes as a result of reduction of intrachain disulfide bonds so that aggregation became unfavorable. Moreover, the dissociation by urea or by 2-mercaptoethanol was found to be irreversible. The origin of the macromolecular aggregate of corticotropin-beta-lipotropin common precursor remains obscure.
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PMID:Characterization of a macromolecular aggregate of ovine pituitary corticotropin-beta-lipotropin common precursor. 626 48

The role of antigen concentration on the immunosuppressive effect of adrenocorticotropin (ACTH) was tested in 6-week-old White Rock chickens that were immunized i.v. with 1 ml of heat-treated Salmonella pullorum at packed cell volume concentrations of .06 to .00015%, At 16 and 10 hr before the antigen (Ag) injection, the birds received either 4 IU . 100 g body wt-1 of ACTH i.m., or the gelatin (Gel) vehicle. Total, 2-mercaptoethanol sensitive (2-MES), and 2-mercaptoethanol resistant (2-MER) agglutinin antibody titers were determined. The ACTH significantly suppressed total agglutinin titers with the lower Ag concentrations (.0015 and .00015%) but not with the higher Ag concentrations. The ACTH significantly suppressed 2-MES titers only when Ag concentrations were low but suppressed 2-MER titers regardless of Ag concentration. The results indicated that there may be critical Ag concentrations capable of inducing maximal humoral antibody responses in moderate environments but which allow these responses to be suppressed by environments that stimulate increased pituitary-adrenal activity.
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PMID:Concentration of Salmonella pullorum antigen and the immunosuppressive effect of adrenocorticotropin in growing chickens. 630 89

In three experiments, 6- to 7-week-old chickens were exposed to one or two standard heating episodes and were injected immediately afterward with different concentrations of heat-killed Salmonella pullorum antigen (Ag) or phosphate-buffered saline. The standard heat episode consisted of three .5-hr exposures of 44 to 46 C with .5-hr periods of 22 C between exposures. Nonheated chickens were maintained at 22 C. When two heating episodes were used, there was a 12-hr interval between episodes. Sera from blood collected at 0 through 15 days postimmunization (PI) were titrated for total agglutinins and assayed for corticosteroids in all three experiments. Additionally, in Experiment 3, sera were titrated for 2-mercaptoethanol-resistant (2-MER) antibody. Total agglutinins were suppressed from 5 through 13 days PI by one heating episode in birds receiving lower doses of Ag but not in those receiving higher doses. When birds were exposed to two heat episodes, 12 hr apart, total agglutinin titers were suppressed in birds receiving the low Ag dose during the induction phase (4 to 5 days PI) only. During the declining phase (7 to 14 days PI), the effect was reversed, and titers were significantly lower in heated birds receiving the higher dosage. These results are similar to those previously obtained with ACTH (adrenocorticotropin). Determination of 2-MER antibody indicated that IgM was probably suppressed during the induction of the immune response but that IgG was suppressed during the declining phase of the response. Serum corticosteroid concentrations were significantly increased immediately after exposure to high temperature.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Interaction of high temperature and Salmonella pullorum antigen concentration on serum agglutinin and corticosteroid responses in white rock chickens. 653 35

Ovine corticotropin-beta-lipotropin common precursor was purified to homogeneity from commercial frozen ovine pituitary glands. A crude preparation was obtained following a procedure published elsewhere (Lee, T.H. and Lee, M.S. (1977) Biochemistry 16, 2824-2829) and was purified by gel filtration on Sephadex G-200 in the presence of 0.5% SDS and 0.1% 2-mercaptoethanol, and under an atmosphere of nitrogen. The gel filtration was repeated once. The partially purified preparation obtained from the second Sephadex G-200 gel filtration was further fractionated by preparative SDS-acrylamide gel electrophoresis, using immunoprecipitated and electrophoretically purified [125I]corticotropin-beta-lipotropin common precursor as a marker. The preparation was judged homogeneous by the appearance of a single protein band in analytical SDS-acrylamide gel electrophoresis, which exhibited both corticotropin and beta-lipotropin immunoreactivities, and a single symmetrical peak in high-pressure liquid chromatography on a reverse phase C18 column. The isolated ovine corticotropin-beta-lipotropin common precursor possessed specific activities of 116 micrograms of immunoreactive corticotropin and 210 micrograms of immunoreactive beta-lipotropin per mg of protein, equivalent to 89 and 62% of theoretical values, respectively. The amino acid composition of the homogeneous preparation was determined.
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PMID:Isolation of corticotropin-beta-lipotropin common precursor from ovine pituitary glands. 674 90

CISP (corticotropin-induced secreted protein) is a secreted protein recently purified in our laboratory from the conditioned medium of ACTH-treated bovine adrenocortical cells. Partial amino acid sequencing of CISP revealed homology with thrombospondins (TSPs), a family of adhesive proteins and in particular with TSP2. We report here the characterization of the molecular structure of CISP. Analysis of CISP by polyacrylamide gel electrophoresis in the absence or presence of SDS indicated an apparent molecular mass approximately equal to 600 kDa for the unreduced protein and an apparent molecular mass of 195 kDa after reduction by 2-mercaptoethanol. The sedimentation coefficient of CISP determined by ultracentrifugation on sucrose gradients was shifted from 9.7 S in the absence to 5.7 S in the presence of 2-mercaptoethanol. These data are consistent with a trimeric organization of the CISP molecule in which 195-kDa monomers would be linked together by disulfide bonds. The trimeric structure of CISP could be observed by rotary shadowing/electron microscopy, where CISP appeared to be composed of three equally electron-dense nodules and of a fourth nodule formed by the close association of three smaller fragments. The overall size of the molecule was 60 nm. We also observed that CISP is sulfated and glycosylated. Using glycosylation inhibitors, we could determine that CISP is synthesized as a 175-kDa core protein, is then matured into a 190-kDa high-mannose form and secreted as a 195-kDa mature protein. Inhibition of sulfation by chlorate did not prevent CISP secretion, whereas inhibition of glycosylation by tunicamycin blocked it. Taken together, these data indicate that the TSP2-related CISP molecule presents both structural and functional properties very similar to those of TSP1. CISP differs greatly, however, from TSP1 by the inducibility of its synthesis by cAMP.
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PMID:The molecular structure of corticotropin-induced secreted protein, a novel member of the thrombospondin family. 839 19