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Titolo:
BIOCHEMICAL AND BIOPHYSICAL COMPARISON OF NATIVE AND CHEMICALLY SYNTHESIZED PHOSPHOLAMBAN AND A MONOMERIC PHOSPHOLAMBAN ANALOG
Autore:
MAYER EJ; MCKENNA E; GARSKY VM; BURKE CJ; MACH H; MIDDAUGH CR; SARDANA M; SMITH JS; JOHNSON RG;
Indirizzi:
MERCK SHARP & DOHME RES LABS,DEPT PHARMACOL,WP44-L206 W POINT PA 19486 MERCK SHARP & DOHME RES LABS,DEPT PHARMACOL W POINT PA 19486 MERCK SHARP & DOHME RES LABS,DEPT MED CHEM W POINT PA 19486 MERCK SHARP & DOHME RES LABS,PHARMACEUT RES DEPT W POINT PA 19486 MERCK SHARP & DOHME RES LABS,DEPT BIOL CHEM W POINT PA 19486
Titolo Testata:
The Journal of biological chemistry
fascicolo: 3, volume: 271, anno: 1996,
pagine: 1669 - 1677
SICI:
0021-9258(1996)271:3<1669:BABCON>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARDIAC SARCOPLASMIC-RETICULUM; MONOCLONAL-ANTIBODY; CALCIUM-PUMP; CA-2+ PUMP; PURIFIED PHOSPHOLAMBAN; PHOSPHOLIPID-VESICLES; SECONDARY STRUCTURE; CIRCULAR-DICHROISM; PROTEIN; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
E.J. Mayer et al., "BIOCHEMICAL AND BIOPHYSICAL COMPARISON OF NATIVE AND CHEMICALLY SYNTHESIZED PHOSPHOLAMBAN AND A MONOMERIC PHOSPHOLAMBAN ANALOG", The Journal of biological chemistry, 271(3), 1996, pp. 1669-1677

Abstract

Phospholamban (PLB) was rapidly isolated from canine cardiac sarcoplasmic reticulum using immunoaffinity chromatography and prepared by solid phase peptide synthesis, The two proteins are indistinguishable when analyzed by SDS-polyacrylamide gel electrophoresis and exhibit pentameric oligomeric states, They are similarly detected on Western blots,are phosphorylation substrates, have identical amino acid compositions that directly reflect their predicted values, yield the same internal amino acid sequences upon CNBr digestion, and have molecular mass values agreeing with the expected value (similar to 6123 Da). Native andsynthetic PLB reduced the calcium sensitivity of Ca2+ ATPase, which is reversed by anti-PLB antibody, A Cys-to-Ser PLB analog, where the cysteines (36, 41, and 46) were substituted by serines, is monomeric on SDS polyacrylamide gel electrophoresis, can be phosphorylated, and is recognized by polyclonal antisera, PLB migrates with a sedimentation coefficient of 4.8 S in sedimentation velocity ultracentrifugation experiments, whereas Cys-to-Ser PLB does not sediment, consistent with a monomeric state, Circular dichroism spectral analysis of PLB indicates about 70% alpha-helical structure, whereas Cys-to-Ser PLB manifests only about 30%. Because the physiochemical properties of native and synthetic PLB appear identical, the more readily available synthetic protein should be suitable for more extensive structural studies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 09:50:20