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Molecular cloning and characteristics of allele variants (GATA)n, the microsatellite locus Du281 of parthenogenetic caucasian rock lizard (Darevskia unisexualis) genome.

Korchagin, V I; Churikov, N A; Tokarskaya, O N; Sevast'yanova, G A; Filippovich, Yu B; Ryskov, A P.

Dokl Biochem Biophys ; 394: 46-8, 2004.

Artículo en Inglés | MEDLINE | ID: mdl-15116568

Asunto(s)

Alelos , Variación Genética , Genoma , Lagartos/genética , Repeticiones de Microsatélite/genética , Animales , Secuencia de Bases , Clonación Molecular , Datos de Secuencia Molecular , Partenogénesis

Isolation, purification, and properties of cysteine proteinase from Bombyx mori L. eggs.

Yarygin, D V; Klunova, S M; Filippovich, Yu B.

Biochemistry (Mosc) ; 68(1): 63-7, 2003 Jan.

Artículo en Inglés | MEDLINE | ID: mdl-12693978

RESUMEN

Silkworm moth (bombyx) egg cysteine proteinase with maximal activity at pH 3.0 was purified by chromatography and isoelectrofocusing. On SDS-electrophoresis in polyacrylamide gel the purified enzyme showed a single band of molecular mass 50 kD. Isoelectrofocusing revealed that the bombyx egg cysteine proteinase exists in two forms with pI values of 5.95 and 6.43, respectively. The enzyme activity was sensitive to inhibition by iodoacetamide and p-chloromercuribenzoate but resistant to EDTA, pepstatin, and phenylmethylsulfonyl fluoride. The cysteine proteinase hydrolyzes storage proteins of bombyx eggs but it was inactive with respect to N-benzoyl-D,L-arginine-p-nitroanilide (BAPNA). It is a cathepsin L-like enzyme.

Asunto(s)

Bombyx/enzimología , Cisteína Endopeptidasas/química , Cisteína Endopeptidasas/aislamiento & purificación , Óvulo/enzimología , Animales , Cromatografía en Gel , Cisteína Endopeptidasas/metabolismo , Inhibidores de Cisteína Proteinasa/farmacología , Electroforesis en Gel de Poliacrilamida , Femenino , Concentración de Iones de Hidrógeno , Peso Molecular

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