Oxygen-binding Properties of Complexes
between Dextran and Pyridoxal
5-Phosphate-Modified Porcine Hemoglobin
HONG Min,SONG Wen-Jun,LI Shi-Yun and YUAN Zhong-Yi
( Shanghai Institute of Biochemistry,the Chinese Academy of Sciences,Shanghai
200031,China )
Abstract It was demonstrated by oxygen
equilibrium curve that the pyridoxal 5-phosphate(PLP) modified porcine
deoxyhemoglobin(pHbβ) 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 pHbβ and p-toluenesolfonyl chloride-actived dextran.
The oxygen affinity of Dx-pHbβ was high than that of pHbβ,but still lower than
that of pHb. Judged by cellulose acetate film electrophoresis,the mobility of
Dx-pHbβ was apparently different from that of pHbβ. Dx-pHbβ has characterized
absorbance peak in UV spectrum,which can be used to analysis the binding ratio
between Dx and pHbβ.
Key Words Porcine hemoglobin；pyridoxal 5-phosphate；dextran
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