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Volumn 11, Issue 1, 2002, Pages 129-136

Hemoglobin Porto Alegre forms a tetramer of tetramers superstructure

Author keywords

Disulfide bridge; Hemoglobin; Oxygen transport; Structure oligomer

Indexed keywords

CYSTEINE; HEMOGLOBIN VARIANT; OLIGOMER; TETRAMER; UNCLASSIFIED DRUG;

EID: 0036136635     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.35702     Document Type: Article
Times cited : (21)

References (25)
  • 13
    • 0032052760 scopus 로고    scopus 로고
    • Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins
    • (1998) J. Biol. Chem. , vol.201 , pp. 1073-1084
    • Riggs, A.F.1
  • 16
    • 0022000499 scopus 로고
    • A new hemoglobin variant, hemoglobin Nunobiki [α141 (HC3) Arg→Cys]. Notable influence of the carboxy-terminal cysteine upon various physico-chemical characteristics of hemoglobin
    • (1985) J. Clin. Invest. , vol.75 , pp. 695-701
    • Shimasaki, S.1
  • 21
    • 0018589643 scopus 로고
    • Exchange of α-β dimers of hemoglobin Porto Alegre [β9(A6) Ser leads to Cys] and normal hemoglobin in the formation of the disulfide polymer
    • (1979) An. Acad. Brasil. Cienc. , vol.51 , pp. 757-764
    • Tondo, C.V.1    Reishl, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.