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Volumn , Issue 29, 2006, Pages 3131-3133

Construction of glycosylated myoglobin by reconstitutional method

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; GALACTOSE; HEMOPROTEIN; MYOGLOBIN;

EID: 33746275566     PISSN: 13597345     EISSN: None     Source Type: Journal    
DOI: 10.1039/b606060a     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 0001094662 scopus 로고    scopus 로고
    • and references therein
    • R. A. Dwek Chem. Rev. 1996 96 683
    • (1996) Chem. Rev. , vol.96 , pp. 683
    • Dwek, R.A.1
  • 18
    • 2442679453 scopus 로고    scopus 로고
    • It has been proposed that masking the porphyrin moiety is important to avoid any non-specific binding to a cell due to the hydrophobicity of the porphinoids.
    • O. Hayashida I. Hamachi J. Org. Chem. 2004 69 3509
    • (2004) J. Org. Chem. , vol.69 , pp. 3509
    • Hayashida, O.1    Hamachi, I.2
  • 26
    • 33746319748 scopus 로고    scopus 로고
    • It is conceivable that we might have observed not only the reconstituted myoglobin-lectin complex but also the binding of the free galactohemin to the lectin, leaving apomyoglobin in solution. However, the remarkable release of the galactohemin from the protein matrix during the purification procedures has never been detected. This finding suggests that the binding of the galactohemin to apomyoglobin is sufficiently strong (see also reference 15) and the complex composed of the reconstituted myoglobin and the lectin will be dominant
    • It is conceivable that we might have observed not only the reconstituted myoglobin-lectin complex but also the binding of the free galactohemin to the lectin, leaving apomyoglobin in solution. However, the remarkable release of the galactohemin from the protein matrix during the purification procedures has never been detected. This finding suggests that the binding of the galactohemin to apomyoglobin is sufficiently strong


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.