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Volumn 35, Issue 7, 2000, Pages 535-538

Effect of thermal denaturation of albumin microspheres on their water-solubility and enzymatic degradation

Author keywords

Albumin; Enzymatic degradation; Microspheres; Water solubility

Indexed keywords


EID: 0002911547     PISSN: 05134870     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (10)
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    • (1999) Chin J Pharm (In Chinese) , vol.30 , Issue.3 , pp. 113-116
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    • Secondary structure of diphtheria toxin and fragments interacting with acidic liposomes studied by polarized infrared spectroscopy [J]
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  • 8
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    • Analyses by Fourier transform infrared spectroscopies of protein structures of soluble NADH-cytochrome b5 reductases prepared by site-directed mutagenesis: Comparison with ferredoxin-NADP + reductase [J]
    • Satoshi Y, Toshitsuga Y, Komei S, et al. Analyses by Fourier transform infrared spectroscopies of protein structures of soluble NADH-cytochrome b5 reductases prepared by site-directed mutagenesis: comparison with ferredoxin-NADP + reductase [J]. Biospectroscopy, 1997,3(3):215-223.
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    • Satoshi, Y.1    Toshitsuga, Y.2    Komei, S.3
  • 9
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    • Characterization of the secondary structure and assembly of the transmembrane domains of trypsinized Na,K-Atpase by Fourier transform infrared spectroscopy [J]
    • Thomas H, Mikael E, Derrk M. Characterization of the secondary structure and assembly of the transmembrane domains of trypsinized Na,K-Atpase by Fourier transform infrared spectroscopy [J]. J Biol Chem , 1997,272(41): 25685-25692.
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  • 10
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    • Anthony, F.1    Yapel, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.