Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme.

The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.

The crystal structure of tortoise egg-white lysozyme at 6 A resolution.

Lysozyme extracted from the egg-white of tortoise, the first example of a reptilian lysozyme to have been purified, has been crystallized and its tertiary structure determined at low resolution by X-ray analysis. This structure is shown to be closely homologous to that of hen egg-white lysozyme. The crystals of tortoise egg-white lysozyme contain a large proportion of liquid and the X-ray map shows that this forms large channels through the crystals into which the active sites of the enzyme molecules open.

Crystallization of the Fv fragment of mouse myeloma protein M315.

The Fv fragment of mouse myeloma protein M313 was crystallized from poly(ethylene glycol) solution in the form of monoclinic crystals, space group C2 and unit cell dimensions a = 5.96 nm (59.6 A), b = 5.

The level of antibodies to the proteins of cow's milk in the serum of normal human infants.

The coated tanned red cell technique has been used to measure the level of serum antibody in normal infants to the proteins of cow's milk. In 286 sera of infants between the ages of 7 and 97 weeks titres up to 1000 were found with the mode around 64. This distribution was quite different from that found with adult and infant cord sera.