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Titolo:
SOLID-PHASE PEPTIDE-SYNTHESIS AND BIOLOGICAL-ACTIVITY OF BOVINE THYMOPOIETIN-II (BTP-II)
Autore:
SMITH DD; CONLON JM; PETZEL J; CHEN L; MURPHY RF; MORLEY BJ;
Indirizzi:
CREIGHTON UNIV,SCH MED,DEPT BIOMED SCI,2500 CALIFORNIA PLAZA OMAHA NE68178 BOYS TOWN NATL RES HOSP OMAHA NE 68131
Titolo Testata:
International journal of peptide & protein research
fascicolo: 2, volume: 44, anno: 1994,
pagine: 183 - 191
SICI:
0367-8377(1994)44:2<183:SPABOB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCE; LYMPHOCYTE-T TRANSFORMATION; POLYPEPTIDE HORMONE; UREMIC PATIENT; THYMUS; INTERACTS; RECEPTORS; MUSCLE; CELLS;
Keywords:
BOVINE THYMOPOIETIN II; NICOTINIC ACETYLCHOLINE RECEPTORS; PEPTIDE MAPPING; SOLID-PHASE PEPTIDE SYNTHESIS; THYMIC PEPTIDES; BETA-ASPARTYL SHIFT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
D.D. Smith et al., "SOLID-PHASE PEPTIDE-SYNTHESIS AND BIOLOGICAL-ACTIVITY OF BOVINE THYMOPOIETIN-II (BTP-II)", International journal of peptide & protein research, 44(2), 1994, pp. 183-191

Abstract

Bovine thymopoietin (bTP), a 49 amino acid polypeptide, was synthesized using Merrifield's solid-phase peptide synthesis methodology. The polypeptide was purified using anion-exchange chromatography and reversed-phase HPLC and characterized by mass spectrometry and amino acid analysis of the full-length peptide and of products derived from digestion with Staphylococcus aureus V8 protease. The biological activity of the synthesized product was tested in several assay systems. SyntheticbTP was found to induce the expression of Thy 1.2 antigen on T-lymphocytes from athymic mice, in agreement with previous studies on the biological activity of endogenous bTP. Biological activity at skeletal muscle and neuronal nicotinic acetylcholine receptor sites, as reported by others for bTP, could not be confirmed in our studies. The absence of biological activity at nicotinic receptor sites may be related to the results of a recent report demonstrating the presence of a cobratoxin-like molecule in preparations of natural bTP. These data indicate that synthetic peptides have an important role for the evaluation of the specificity of the biological activity of polypeptides. (C) Munksgaard 1994.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 06:27:40