Proceedings o f the Society for Experimental Biology 143

PROCEEDINGS OF THE FIFTEENTH MEETING OF THE SOCIETY FOR 
EXPERIMENTAL BIOLOGY, 30th NOVEMBER, 1955

A lkali Resistant H aemoglobins F rom Normal and Sickle C ell Bloods, 
by C. G. Anderson (South African Institute fo r Medical Research, Johannesburg).

It is well recognised that haemoglobin from patients with sickle cell anaemia 
contains between 2 and 25 per cent of alkali resistant haemoglobin (Itano, 1953). 
It is accepted that alkali resistant or foetal haemoglobin, F, has an electrophoretic 
mobility very close to that of normal adult haemoglobin, A, whilst sickle haemoglobin, 
S, has a mobility in veronal buffer, pH 8.6, considerably lower than has A. In spite 
of this, haemoglobin from sickle cell anaemia patients shows only the single slow 
peak of S and no peak corresponding to F can be seen, in agreement with the original 
findings of Pauling et al. (1949), and with those of Singer et al. (1951), and of Bergren 
et al. (1954), although Singer and Fisher (1953) and Motulsky et al. (1954) claim that 
the two can be distinguished.

In an attempt to elucidate this discrepancy alkali resistant haemoglobin was 
prepared from normal and sickle haemoglobins by the usual treatment with dilute 
sodium hydroxide solution, precipitation of the denatured haemoglobin with ammo­
nium sulphate and dialysis of the filtrate to remove excess ammonium sulphate. 
Each alkali resistant haemoglobin had the mobility characteristic of the original 
haemoglobin from which it was prepared, that is slow from S and fast from A. When 
alkali resistant haemoglobin from A was mixed with untreated S and submitted to 
electrophoresis a single S peak was obtained; conversely a mixture of alkali resistant 
haemoglobin from S with untreated A had the mobility of A. A mixture of alkali 
resistant haemoglobin from A and S moved as a single peak with an intermediate 
mobility. European or Bantu cord blood haemoglobins showed a single peak with the 
mobility of normal adult haemoglobin, as did the alkali resistant fractions prepared 
from them. However, when alkali resistant haemoglobin from cord blood was mixed 
with untreated S haemoglobin the mixture had the mobility of S.

These facts suggest that the alkali resistant haemoglobins from S and A are not 
different substances as the initial observation might indicate, but may be a single 
compound which is capable of forming complexes (cf. Anderson and Griffiths, 1954) 
with either normal or sickle haemoglobins and which retain the mobility of the native 
haemoglobin.

REFERENCES
A nderson, C. G., and G riffiths, S. B. (1954). Nature, 174, 928.
Bergren, W. R., Sturgeon, P., and Itano, H. A. (1954). Rev. Haentat, 12, 160.
It a n q , H. A. (1953). Science, 117, 89.
Motulsky, A. G., Paul, M. H., and D urrum, E. L. (1954). Blood, 9, 897.
Pauling, L., Itano, H. A., Singer, S. J., and W ells, I, C. (1949). Science, 110, 543.
Singer, K., C hernoee, A. I., and Singer, L. (1951). Blood, 6, 413.
Singer, K., and F isher, B. (1953). J . Im I>. Clin. Med., 42, 193.

E-Amino G roups op H uman Dentine Collagen, by C. C. Solomons and J. T. Irving 
Joint Dental Research Unit o f the Council for Scientific and Industrial Research 
and the University o f the Witwatersrand, Johannesburg).

This work describes the change in the number of free e-amino groups of human 
dentine collagen when treated with demineralizing agents.

0-5 g. samples of root dentine in the form of small cubes were decalcified at 4°C