Oxygen-binding Properties of Complexes between Dextran and Pyridoxal 5-Phosphate-Modified Porcine Hemoglobin.
It was demonstrated by oxygen equilibrium curve that the pyridoxal 5-phosphate(PLP) modified porcine deoxyhemoglobin(pHbbeta) had lower oxygen affinity than that of stroma-free porcine hemoglobin(pHb). Accourding to analysis of SDS-PAGE, the porcine hemoglobin derivatives were not cross-linked between its subunits. A conjugate was synthesized between pHbbeta and p-toluenesolfonyl chloride-actived dextran. The oxygen affinity of Dx-pHbbeta was high than that of pHbbeta, but still lower than that of pHb. Judged by cellulose acetate film electrophoresis, the mobility of Dx-pHbbeta was apparently different from that of pHbbeta. Dx-pHbbeta has characterized absorbance peak in UV spectrum, which can be used to analysis the binding ratio between Dx and pHbbeta.
Shanghai Institute of Biochemistry, the Chinese Academy of Sciences, Shanghai 200031, China. zhongyi@sunm.shcnc.ac.cn
Min
M
Hong
Wen-Jun
WJ
Song
Shi-Yun
SY
Li
Zhong-Yi
ZY
Yuan