Rapid Demonstration of A<sub>2</sub>Hemoglobin By Means of Agar Gel Electrophoresis

Yakulis, Vincent; Heller, Paul; Josephson, Aaron M.; Singer, Lily

doi:10.1093/ajcp/34.1.28

Cited by 27 publications

(3 citation statements)

References 6 publications

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“…Coagulation studies were performed in 52 patients with homozygous sickle cell disease. The diagnosis was confirmed in all patients by agar gel electrophoresis of hemoglobin at pH 8.6 (26) . When S-D disease was suspected, the electrophoresis was repeated at pH 6.2.…”

Section: Methodsmentioning

confidence: 76%

Impaired Fibrinolysis in Sickle Cell Disease

Green¹,

Kwaan²,

Ruiz³

1970

Thromb Haemost

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SummaryCoagulation studies were performed in 52 patients with sickle cell disease during asymptomatic periods and during episodes of crisis and infection. Platelet counts averaged 473,000, 469,000, and 461,000 per mm3 in these 3 groups, and factor VIII concentrations were elevated in all. Fibrinogen was increased to the same extent in both sickle cell and non-sickle cell patients with infection. Fibrinolytic activity, as measured by euglobulin lysis times and zones of lysis on fibrin plates, was markedly reduced during periods of infection in sickle cell patients but not in non-sickle patients. Impairment of fibrinolysis in most patients was not on the basis of overutilization or consumption, since no decrease in the levels of clotting factors or plasminogen was observed. It was suggested that generalized intravascular sickling in these patients may have caused widespread endothelial damage, resulting in decreased production of plasminogen activator.In addition, several sickle cell patients with infection were found to possess elevated levels of an inhibitor directed against urokinase.

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Section: Methodsmentioning

confidence: 76%

Impaired Fibrinolysis in Sickle Cell Disease

Green¹,

Kwaan²,

Ruiz³

1970

Thromb Haemost

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“…Unless extremely pure Hb was used for immunization, the resulting antiserum contained antibodies to non-hemoglobin proteins (NHPs) which were known to disturb species-specificity of the anti-Hb (Suyama et al 1968). Human NHP has been analyzed by electrophoresis using Tiselius apparatus (Stern et al 1945), agar gel (Yakulis et al 1960), starch gel (Haut et al 1962) and polyacrylamide gel (Sawamura 1969;Sagisaka et al 1977). ohya (1970) prepared rabbit antiserum to human carbonic anhydrase (CA), a main ingredient of NHP, isolated from lysate by the chroloform ethanol method (Huennekens et al 1957).…”

mentioning

confidence: 99%

Human specific antigens and species difference in non-hemoglobin proteins of red cell lysate.

Sagisaka¹,

Yamashita²,

Iwasa³

et al. 1981

Tohoku J. Exp. Med.

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Non-hemoglobin proteins (NHPs) of 12 species of mammalian were effectively isolated from red cell lysates with CM-Sephadex chromatography. Polyacrylamide gel disc electrophoresis demonstrated that human and monkey NHPs had 13 and 11 bands, respectively, but guinea pig and swine two to three bands. Rabbit anti-human NHP reacted with monkey, bovine, canine and badger as well as human. Absorption of the anti-NHP with monkey NHP resulted in preparing human specific anti-NHP. The specific antiserum gave two bands locating near the origin in immunoelectrophoresis. Human specific antigens were prepared by affinity chromatography with the anti-NHP. The antigens were composed of three bands, two of which had slightly faster mobility than carbonic anhydrase and the other migrated fastly on disc electrophoresis. These bands were proved to have neither LDH nor esterase activity.hemolysate; non-hemoglobin protein; human specific antigen; species difference

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“…The starch block and agar gel electrophoretic methods for A2 are technically cumbersome and impractical for the routine clinical laboratory, although Yaukulis ct al. (5), Goldberg (6), and Zak et al (7) have employed agar gel electrophoresis for rapid separa tion of A2 hemoglobin. Goldberg (B,9) has reported excellent separation of A2 with starch-gel electrophoresis, employing dis continuous buffer systems.…”

mentioning

confidence: 99%