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Titolo:
BIOCHEMICAL-PROPERTIES OF ATTACHMENT REGION BINDING-PROTEIN ARBP
Autore:
VONKRIES JP; ROSORIUS O; BUHRMESTER H; STRATLING WH;
Indirizzi:
UNIV KRAKENHAUS EPPENDORF,INST PHYSIOL CHEM,MARTINSTR 52 D-20246 HAMBURG GERMANY UNIV KRAKENHAUS EPPENDORF,INST PHYSIOL CHEM D-20246 HAMBURG GERMANY
Titolo Testata:
FEBS letters
fascicolo: 2, volume: 342, anno: 1994,
pagine: 185 - 188
SICI:
0014-5793(1994)342:2<185:BOARBA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
SCAFFOLD; CHROMATOGRAPHY; PURIFICATION; ORDER; SIZE;
Keywords:
CHROMATIN ORGANIZATION; ARBP; DNA BINDING DOMAIN; SEDIMENTATION COEFFICIENT; STOKES RADIUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Vonkries et al., "BIOCHEMICAL-PROPERTIES OF ATTACHMENT REGION BINDING-PROTEIN ARBP", FEBS letters, 342(2), 1994, pp. 185-188

Abstract

ARBP (attachment region binding protein) is an abundant nuclear protein that specifically binds to matrix/scaffold attachment regions (MARs/SARs). Here we show by gel filtration and gradient sedimentation thatARBP has an elongated shape. The sedimentation coefficient was determined as only 2.1 S. Furthermore, limited proteolysis of ARBP in situ (in isolated nuclei) with several proteases generated limiting resistant peptides from 14.5 to 18 kDa, that retained the ability to bind MARsspecifically. This indicates that these peptides encompass the DNA binding domain of ARBP.

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Documento generato il 18/09/20 alle ore 10:46:40