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Biomedical subjects

Min Hong

Publications and source records attributed to Min Hong.

22 records · Page 2Linked to original sources
PubMed2000

Preparation of Inositol Tetrakisphosphate and Its Application in Modification of Porcine Hemoglobin.

Modification of hemoglobin using inositol tetrakisphosphate (IP(4)) can improve the oxygen affinity of hemoglubin. Phytase was extracted from wheat bran and purified by ammonium sulphate fractionation, followed by Sephadex G-50 gel filtration and Mono Q chromatography. The purified phytase was used for hydrolysis of phytic acid under controled conditions. IP(4), as a major composition of the hydrolysate, was further purified on resin 714 column. The purified IP(4) was oxidized by periodate to obtain dialdehyde-IP(4). By the reaction between the aldehyde group of IP(4) derivative and the amino group of porcine hemoglobin (pHb), pHb-IP(4) conjugate was formed and was found to have better ability of O(2) binding and releasing than the native hemoglobin.

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PubMed1999

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.

Journal Article↗
PubMed1999

Oxidized Raffinose Intramolecular Cross-linking of Porcine Hemoglobin Effects on Its Structure and Function.

Periodate-oxidized raffinose is utilized to modify porcine oxyhemoglobin and deoxyhemoglobin, respectively. These modified protein derivatives showed special characteristics that it can resist the dissociation of alpha(2)beta(2) tetramer in comparison with natural proteins. According to the analysis in SDS-PAGE and reverse phase HPLC, the two porcine hemoglobin derivatives are all intramolecular linked proteins and the cross-linking sites lie between the two beta subunits. No eminent differences were found in the UV-VIS absorption spectrum between natural and modified proteins. However, after calibration for protein concentration, the emission of modified porcine deoxyhemoglobin is much weaker than the modified oxyhemoglobin and the natural protein. Furthermore, the porcine hemoglobin derivatives' characteristics of the oxygen affinity and Auto-oxidized rate also show significant differences with natural protein. The possible application of these porcine hemoglobin derivatives in the preparation of hemoglobin-based blood substitutes is discussed.

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