Assumption of a water-impermeable coat on bacterial spores is inconsistent with known permeabilities of organic materials. A low water content may arise through compressive contraction of the cortex during spore maturation.

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A new spore phenomenon is described in which induction of increased heat resistance occurs during the process of heating. In buffered environments the acid form of dormant mature bacterial spores shows a temperature dependent adaptation to heat which is correlated with the rate of uptake of Ca(OH)(2) by titration at constant p(H) in neutral salt solution.

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Amino acid analyses of normal wools of several breeds and geographical origins are presented as evidence of the normal variation of composition. Some samples were from lots used for detailed comparative studies of fiber properties and processing behavior. A mohair sample was found to be similar to wool in composition. White Leghorn chicken feather keratin differed from wool in yielding larger amounts of serine and proline. Feather had characteristically smaller amounts of cystine and glutamic acid. Heterogeneity of wool and feather keratins was shown by differences in amino acid composition of fractions prepared by treatment with acid, by mechanical separation, or by partial solubilization in aqueous alcohol. Feather differs from wool in having readily separable fractions differing greatly in content of histidine, lysine, and methionine. These fractions also differ appreciably in their content of several other amino acids.

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