Hemoglobin from the cobra snake, Naja naja naja, was isolated and its chains separated on a CM-cellulose column. The separation profile revealed an α and two β chains having the molar proportions of [ α ] 2 ,[ β 1 ] 1 ,[ β 2 ] 1 . The N-terminal amino acid sequence of the intact chains and of the CNBr peptides were carried out. The β 2 chain was found to be heterogeneous comprising a minor component amounting to 11%. This later showed changes at two positions 9 and 14 in the first 30 residues sequenced.

The fungus Aspergillus flavipes was grown on a Czapeck sucrose medium; the biomass so obtained was treated with high concentration of sucrose to release intracellular metabolites. Sephadex G-75 chromatography of the latter yielded a pure protein having anti-trypsin activity in vitro.

A small protein (M r about 14 000) rich in cysteine/half-cystine has been isolated from camel milk by exclusion chromatography and reverse-phase high-performance liquid chromatography. The N-terminal amino acid sequence shows a region with several positional identities with α and β-caseins, which however lack cysteine residues; postions 16–20 are identical and involve the serine residues that have been found to be phosphorylated in β-caseins.