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Short glycopeptides were prepared from bovine colostral K-casein treated with cyanogen bromide and proteases (pronase P and thermolysin), followed by gel filtrations and ion exchange chromatography. It was confirmed by Edman degradation that glycopeptide I among short glycopeptides obtained was homogeneous. From the effect of alkali treatment, it was assumed that three polysaccharide chains of glycopeptide I were attached to the peptide chain through OH groups of threonines. By chemical procedures and carboxypeptidase P treatment, the amino acid sequence of glycopeptide [ was established to be Ser-Gly-Glu-Pro-Thr-Ser-Thr-Pro-Thr-Thr-Glu-Ala-Val. Threonine residues of No. 5, 7 and 9 were bound to the carbohydrate chains through galactosamine. The sugar chain bound to the threonine residue at No.7 contained glucosamine. Glycopeptide I corresponded to residues of No. 127 ~ 139 in K-casein A from normal milk.

Addition of Carbon Tetrachloride to 1-Octene.-This reaction was carried out as described above except that all reagents were doubled and 89.6 g of 1-octene was used in place of allyl alcohol.The mixture was heated in six 45-ml polymerization tubes. The products were 41 g (38.5%) of 1,1,1,3-tetrachlorononane,4•11•12 bp 95-98°( 1.7-2.0 mm), nmd 1.4768, nmr (CC14) 3.2 (2 d, 2, -CH2CCI3), 4.2 (m, 1, -CHC1-), 1.85 (m, 2, -CHjCHCl-), 1.36 (m, 8, -CHj-), 0.9 (t, 3, -CHS), and 5.5 g (4%) of 9,9,11-trichloro-7-heptadecene, bp 170°(2.0 mm), nmD 1.4766, nmr (CC14) 0.9 (t, 3, -CH8), 1.2-1.8 (m, 10, -CHa-), 4 (m, 1, -CHC1-), 5.5 (d, 1, -CH=), 2.7 (d, 2, =CClCHa-). Anal.

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