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Natalya Lebedeva,Elena Malkova,Anatoly Vyugin,Oscar Koifman,Yury Gubarev 한국바이오칩학회 2016 BioChip Journal Vol.10 No.1
Spectral, hydrodynamic and thermochemical studies have been demonstrated that tetraalkoxy substituted zinc(II)phthalocyanines form stable complexes with defatted and nondefatted bovine serum albumin. The phthalocyanines interact with BSA through heteroatoms of their peripheral substitutes. It was found that ZnPc(4-NH-CO-C6H4-OC3H7)4 is located in the protein subdomains IB and IIA whereas ZnPc(4-NHCO- C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4-OC8H17)4 are immobilized on surface of the protein globule at a distance of not greater than 10 nm from the tryptophan residues in the positions 135 and 214 of the protein polypeptide chain. Zinc(II)phthalocyanines (ZnPc(4- NH-CO-C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4- OC8H17)4) increase thermal stability of BSA. Spectral, hydrodynamic and thermochemical studies have been demonstrated that tetraalkoxy substituted zinc(II)phthalocyanines form stable complexes with defatted and nondefatted bovine serum albumin. The phthalocyanines interact with BSA through heteroatoms of their peripheral substitutes. It was found that ZnPc(4-NH-CO-C6H4-OC3 7)4 is located in the protein subdomains IB and IIA whereas ZnPc(4-NHCO- C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4-OC8H17)4 are immobilized on surface of the protein globule at a distance of not greater than 10 nm from the tryptophan residues in the positions 135 and 214 of the protein polypeptide chain. Zinc(II)phthalocyanines (ZnPc(4- NH-CO-C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4-OC8H17)4) increase thermal stability of BSA.