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Titolo:
Primacy structure of two cytolysin isoforms from Stichodactyla helianthus differing in their hemolytic activity.
Autore:
Huerta, V; Morera, V; Guanche, Y; Chinea, G; Gonzalez, LJ; Betancourt, L; Martinez, D; Alvarez, C; Lanio, ME; Besada, V;
Indirizzi:
Ctr Genet Engn & Biotechnol, Prot Struct Dept, Div Phys Chem, Havana, CubaCtr Genet Engn & Biotechnol Havana Cuba pt, Div Phys Chem, Havana, Cuba Univ Havana, Fac Biol, Dept Biochem, Havana, Cuba Univ Havana Havana Cuba iv Havana, Fac Biol, Dept Biochem, Havana, Cuba
Titolo Testata:
TOXICON
fascicolo: 8, volume: 39, anno: 2001,
pagine: 1253 - 1256
SICI:
0041-0101(200108)39:8<1253:PSOTCI>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANEMONE ACTINIA-EQUINA; AMINO-ACID-SEQUENCE; PORE-FORMING TOXIN; SEA-ANEMONE; SECONDARY STRUCTURE; PROTEIN; MUTAGENESIS; ALIGNMENT;
Keywords:
primary structure; secundary structure prediction; sea anemone; cytolysin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
12
Recensione:
Indirizzi per estratti:
Indirizzo: Guanche, Y Ctr Genet Engn & Biotechnol, Prot Struct Dept, Div Phys Chem, POB 6162, Havana, Cuba Ctr Genet Engn & Biotechnol POB 6162 Havana Cuba Havana, Cuba
Citazione:
V. Huerta et al., "Primacy structure of two cytolysin isoforms from Stichodactyla helianthus differing in their hemolytic activity.", TOXICON, 39(8), 2001, pp. 1253-1256

Abstract

Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the yea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behaviorof St-I and St-II, we report here the complete amino acid sequences and the consensus secondary structure prediction of both proteins. The complete determination of St-II primary structure confirms the partial revision of cytolysin III amino acid sequence. All nonconservative changes between St-I and St-II are located at the N-terminal. According to our prediction these changes could be located at the same face of an a-helix during pore formation events and could account for the observed differences in hemolytic activity between St-I and St-II. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 06:33:31