SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS

Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a pH so low that practically none of the SH groups of native hemoglobin and of native lens protein are active. The effect of denaturation on the SH groups of a protein is to extend towards the acid side the pH range of their activity. It is possible to oxidize the iron-porphyrin and the SH groups of hemoglobin independently of each other.     

THE RHEOLOGY OF THE BLOOD : IV. THE FLUIDITY OF WHOLE BLOOD AT 37°C.

In the preceding paper (1b) a formula was developed for the lowering of the fluidity of a medium by a mixture of proteins, given the volume concentration of each and its fluidity-lowering constant. Whole blood is now shown to follow an essentially similar formula, except that the hemoglobin content is taken from the literature as the best available measure of the volume of the blood cells Δ Φ = 0.24H, assuming the fluidity of the medium to be 53 rhes. Age, sex, diet, barometric pressure affect the hemoglobin content of the blood, but the formula may apply to any healthy human blood to about 3 per cent. The shape, number, and size of the blood cells, if known, might help to explain discrepancies as well as the state of oxidation of the blood. In disease the discrepancy becomes much greater, suggesting the possible use of rheology in diagnosis.