DETERMINATION OF THE APPARENT BINDING CONSTANT OF COBALT CARBONIC ANHYDRASE B BY THE KINETIC METHOD

1977 ◽  
Vol 6 (5) ◽  
pp. 475-478 ◽  
Author(s):  
Yoshinori Kidani ◽  
Junzo Hirose
Blood ◽  
1968 ◽  
Vol 32 (5) ◽  
pp. 796-810 ◽  
Author(s):  
DAVID GITLIN ◽  
TERUO SASAKI ◽  
PEKKA VUOPIO

Abstract An immunochemical method for the quantitative determination of specific soluble proteins in individual erythrocytes has been described. Application of the method revealed: 1. From 0.5 to 0.9 per cent of the normal adult erythrocytes studied contained small amounts of γ-chains, from 2.5 to 12.5 µµg. as hemoglobin per cell. 2. In cord blood of normal infants of 38 weeks’ gestation, significant numbers of erythrocytes were found which contained either γ-chains or β-chains or both, independently of carbonic anhydrase B. 3. Once initiated within a given erythrocyte, β-chain synthesis in that cell rapidly approached adult rates. Derepression of carbonic anhydrase B synthesis was independent of derepression of hemoglobin synthesis, and in fetal cells which contained carbonic anhydrase B the amount found was well below that of most adult erythrocytes. 4. In 4 patients homozygous for hemoglobin S and in 2 persons heterozygous for thalassemia, an increase in F hemoglobin was associated with an increase in γ-chain content of individual erythrocytes as well as an increase in the number of erythrocytes containing γ-chains; in 2 patients homozygous for thalassemia, an unusual distribution of cells with increased γ-chain content was observed.


1992 ◽  
Vol 269 (2) ◽  
pp. 273-279 ◽  
Author(s):  
Rafael Jiménez-Prieto ◽  
Antonio Velasco ◽  
Manuel Silva ◽  
Dolores Pérez-Bendito

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