FIBRINO-PEPTIDE 203 2. A peptide appears in the fibrinogen-thrombin system. 3. It is suggested that this hitherto unknown substance should be called 'fibrino-peptide', since it is believed to be derived by splitting off part of the fibrinogen molecule. 4. A method for isolating apparently pure fibrino-peptide is given. 5. The release of fibrino-peptide is correlated with previous results, and the clotting of fibrinogen is discussed in the light of the new finding. Iwish to thank Prof. W. T. Astbury, F.R.S., forthe benefit of discussions, and Dr W. R. Middlebrook for his valuable help in the chromatographic experiments.

No abstract

The total lipids (8.6 %) extracted from whole lupin seeds (Lupinus angustifolius L. var. "Uniwhite") were found to be comprised of triglycerides (71.1 %), phospholipids (14.9%), free sterols (5.2%), glycolipids (3.570, sterol and wax esters (0.5 %), free alcohols (0.4 %), hydrocarbons (0.4 %) and unidentified waxy material (4.0%). The main fatty acids in the total lipid extract were linoleic (48.3 %), oleic (31.2 %), palmitic (7.6%) and linolenic (5.4%). Erucic acid was not present, nor were cyclopropenoid acids. Seed coatings constituted 23.9% of the weight of the whole seeds and contained 1.5 %lipids, the main classes of which were triglycerides (38.4 %), free sterols (28.0 %), phospholipids (9.7 %), glycolipids (9.1 %) and free alcohols (3.7 %). The seed coatings and kernels contained the same fatty acid constituents, but the proportions of oleic, linoleic and linolenic acids were markedly different. p-Carotene was present, although at low concentration. When evaluated on its lipid composition, "Uniwhite" lupin seed appears suitable as a supplement for pig, poultry and stock feeding.

No abstract

I953 a hydrolysate of the DNP derivative of fraction A, showing that the only glycine residues are Nterminal. The results with carboxypeptidase support the conclusion that asparagine is the C-terminal residue of the glycyl chain. In the case of acetylinsulin the liberation was approximately quantitative, assuming that it is present in both the glycyl chains, if one assumes that the molecular weight is 12 000. SUMMARY 1. Fraction A of oxidized insulin was hydrolysed with pepsin ancl chymotrypsin. The resulting peptides were fractionated and their structure investigated. 2. It is concluded that the amino-acid sequence in the glycyl chain of insulin is Gly. Ileu.