Serum albumin is a protective bacterial growth factor; by binding traces of fatty acid in the media it permits initiation of growth by the smallest possible inocula of tubercle bacilli. Each molecule of albumin binds 3 to 6 molecules of oleic acid (1 to 2 per cent of the weight of the albumin) tightly enough to prevent bacteriostasis, and 9 molecules of oleic acid in equilibrium with a saturated neutral solution. The property requires undenatured albumin. Crystalline ß-lactoglobulin has a smaller capacity, and a number of other proteins no perceptible capacity to bind oleic acid.
The inhibitory effect of the commercial product Tween 80 (polyoxyethylene sorbitan monooleate) on the growth of small inocula of tubercle bacilli in liquid media is caused by its content of unesterified oleic acid (0.6 per cent by weight). Purified Tween 80, freed of this contaminating fatty acid, not only permits growth of small inocula, but protects against small amounts of added oleic acid.
The implications of the binding capacity of albumin for its possible physiological significance in the animal body (transport; protection against cytotoxins), and for the structure of the protein, are briefly discussed.