Primary structure of triacetinase — An esterase from cotton seeds IV. Peptides of the chymotryptic and thermolytic hydrolysis of cyanogen bromide fragments of triacetinase

Summary 1. Peptides from a chymotryptic hydrolyzate of cyanogen bromide fragment B-7 have been isolated and characterized. The structure of some peptides of the chymotryptic hydrolyzate have been studied and this has enabled the tryptic peptides to be linked up.2. The peptides of a thermolysin hydrolyzate of cyanogen bromide B-5 have been isolated and characterized. The study of the structure of the thermolysin peptides has permitted the linking of two tryptic peptides.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 248–253, March–April, 1978.     

The force fields of cyanogen halides. III. Cyanogen bromide and cyanogen iodine

Following work determining the force fields of FCN and ClCN a related treatment for BrCN and ICN leads to the force fields indicated in Table 1 and giving the agreement with experiment shown by Tables 3, 4 and 5 for BrCN and Tables 7 and 8 for ICN. Table 6 gives the agreement of B₀ values for all isotopic molecules with r_e values for BrCN of 178.611 and 115.767 pm and for ICN of 199.241 and 115.965 pm for the XC and CN bonds, respectively.     

Primary structure of triacetinase — An esterase from cotton seeds III. Peptides from tryptic hydrolysis

Summary 1. The peptides from tryptic hydrolysis of triacetinase have been isolated and characterized and their amino-acid sequences have been determined.2. On the basis of the results of the determination of the amino-acid sequences of the peptides of the tryptic hydrolyzate the sequence of peptides of the cyanogen bromide hydrolysis of triacetinase has been established or confirmed.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 241–248, March–April, 1978.     

Quaternary structure of cottonseed triacetinase

Summary 1. It has been established that the triacetinase of cotton seeds with mol. wt. 40,000 consists of two active subunits with mol. wt. 20,000, each of which in its turn consists of two protomers with mol. wt. 10,000 bound to one another by lipids.2. The conditions for the dissociation and association of the subunits have been determined. It has been shown by the method of peptide maps that the subunits consists of identical polypeptide chains.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 805–808, November–December, 1976.     

Primary structure of the alanine subunit of ricin T from seeds of the Central Asian castor oil plant. V. Peptides obtained by cyanogen bromide cleavage

The cleavage of the carboxymethylated Ala subunit of ricin T by cyanogen bromide has been performed. Four fragments have been isolated in the individual state by gel filtration and high-voltage paper electrophoresis. The sequence of the cyanogen bromide peptides in the protein chain has been established. Partial structures of three cyanogen bromide fragments have been determined.Institute of Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodynkh Soedinenii, No. 6, pp. 845–848, November–December, 1988.     

Primary structure of the alanine subunit of ricin T from seeds of the Central Asian castor oil plant. V. Peptides obtained by cyanogen bromide cleavage

The cleavage of the carboxymethylated Ala subunit of ricin T by cyanogen bromide has been performed. Four fragments have been isolated in the individual state by gel filtration and high-voltage paper electrophoresis. The sequence of the cyanogen bromide peptides in the protein chain has been established. Partial structures of three cyanogen bromide fragments have been determined.     

Primary structure of the alanine subunit of ricin T from the seeds of the Central Asian castor oil plant VI. Tryptic peptides of the cyanogen bromide fragments B-1, B-2, and B-3

Tryptic hydrolysates of cyanogen bromide fragments B-1, B-2, and B-3 have been studied. As a results, 23 tryptic peptides have been isolated and characterized and the primary structures of 22 of them have been established. Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (371) 120 64 75. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 801–806, November–December, 1998.     

The reaction of monoethanolamine with cyanogen bromide

The reaction of monoethanolamine with cyanogen bromide has been studied. 2-Imino-1,3-oxazolidine has been obtained and its structure has been proved. It has been confirmed that the reaction of cyanamide or calcium cyanamide with organic oxides and their chlorohydrins forms, in the first stage, hydroxyalkyl derivatives of cyanamide which cyclize with the formation of the corresponding 2-iminooxazolidine derivatives. 2-Aminooxazone derivatives are obtained by the tautomerization of the 2-iminooxazolidine derivatives.     

Chemical characterization of the crystalline proteins ofBac. thuringiensis. Cleavage with cyanogen bromide

The crystalline proteins fromBac. thuringiensis of the third and fourth serotypes with a molecular weight of 130,000 have been isolated and carboxymethylated, and their amino acid compositions has been determined. The CM-proteins have been found to be labile in acid media (80% CF₃COOH and 65% HCOOH). Conditions have been found for the cleavage of the CM-protein of the third serotype with cyanogen bromide. A BrCN fragment with a molecular weight of 16,000 has been isolated, the intensity of which in 5% polyacrylamide gel on scanning amounts to about half the intensity of the sum of all the fragments. The aminoacid composition of this fragment has been determined.Institute of Chemistry of the Bashkir Branch, Academy of Sciences of the USSR, Ufa. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 384–386, May–June, 1980.