TY - JOUR
T1 - Plasma Protein Alterations in AIDS and Hemophilia A
AU - Dayal, V. K.
AU - Lea, M. A.
AU - Arkel, Y. S.
PY - 1986/1/1
Y1 - 1986/1/1
N2 - Plasma proteins of patients with AIDS, ARC, hemophilia A, and some viral infections were studied using various electrophoretic techniques, and compared to healthy control subjects. On isoelectric focusing (IEF) gels the most prominent and consistent finding was a marked increase in a basic protein band (AABP) at pI≃9.0 in plasma samples derived from AIDS and hemophilia A patients. Using SDS gels, we noted an increased amount of protein in the 90 KD region in AIDS patients as compared to control subjects. On two dimensional gels (2D gels) basic protein(s) with pI≃8.1-9.0 and molecular weight of approximately 90 KD were noted to be increased. In addition, a basic protein of 27 KD along with two acidic proteins in the low molecular weight region were also elevated in AIDS plasma. Although a limited number of samples were analyzed, it seems probable that a number of proteins are altered in AIDS plasma. AABP stained positive with periodic acid Schiff (PAS) reagent, indicating that it is a glycoprotein. This protein did not bind to an anti-IgG sepharose column, suggesting that it is not an immunoglobulin. The purified protein also did not react with antibody to fibrinogen and hemoglobin β-chain. There are many changes in the plasma protein pattern of AIDS and hemophilia A patients as compared to normal controls.
AB - Plasma proteins of patients with AIDS, ARC, hemophilia A, and some viral infections were studied using various electrophoretic techniques, and compared to healthy control subjects. On isoelectric focusing (IEF) gels the most prominent and consistent finding was a marked increase in a basic protein band (AABP) at pI≃9.0 in plasma samples derived from AIDS and hemophilia A patients. Using SDS gels, we noted an increased amount of protein in the 90 KD region in AIDS patients as compared to control subjects. On two dimensional gels (2D gels) basic protein(s) with pI≃8.1-9.0 and molecular weight of approximately 90 KD were noted to be increased. In addition, a basic protein of 27 KD along with two acidic proteins in the low molecular weight region were also elevated in AIDS plasma. Although a limited number of samples were analyzed, it seems probable that a number of proteins are altered in AIDS plasma. AABP stained positive with periodic acid Schiff (PAS) reagent, indicating that it is a glycoprotein. This protein did not bind to an anti-IgG sepharose column, suggesting that it is not an immunoglobulin. The purified protein also did not react with antibody to fibrinogen and hemoglobin β-chain. There are many changes in the plasma protein pattern of AIDS and hemophilia A patients as compared to normal controls.
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U2 - 10.1089/aid.1.1986.2.309
DO - 10.1089/aid.1.1986.2.309
M3 - Article
C2 - 3814260
AN - SCOPUS:0022910902
VL - 2
SP - 309
EP - 319
JO - AIDS Research and Human Retroviruses
JF - AIDS Research and Human Retroviruses
SN - 0889-2229
IS - 4
ER -