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The primary structure of histone h 1 from sperm of the sea urchin parechinus angulosus 2. sequence of the carboxyl terminal cyanogen bromide peptide and the entire primary structure


, : The primary structure of histone h 1 from sperm of the sea urchin parechinus angulosus 2. sequence of the carboxyl terminal cyanogen bromide peptide and the entire primary structure. European Journal of Biochemistry 104(2): 567-578

The primary structure of sperm histone H1Parechinus was determined. H1Parechinus consists of a polypeptide chain of 248 amino acid residues. The protein consists of 3 domains. Compared to other H1 and H5 histones, there is a very similar hydrophobic central domain and the carboxyl-terminal domain is very rich in lysine and alanine. H1Parechinus is similar to H5 histones in that the carboxyl-terminal domain also contains many arginine residues close to the carboxyl terminus.

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Related references

Strickland, W.N.; Strickland, M.; Brandt, W.F.; Von Holt, C.; Lehmann, A.; Wittmann-Liebold, B., 1980: The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. 2. Sequence of the C-terminal CNBr peptide and the entire primary structure. The primary structure of sperm histone H1Parechinus has been determined. H1Parechinus consists of a polypeptide chain of the following 248 amino acid residues: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser...

Strickland, W.N.; Strickland, M.; de Groot, P.C.; Von Holt, C.; Wittmann-Liebold, B., 1980: The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. 1. Chemical and enzymatic fragmentation of the protein and the sequence of amino acids in the four N-terminal cyanogen bromide peptides. The primary structure of the amino-terminal 84 residues of sperm histone H1Parechinus has been determined. The sequence is: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser-Pro-Arg-Lys-Ala-Ser-Ala-Ser-Pro-Arg...

Strickland, W.N.; Strickland, M.; De-Groot, P.C.; Von-Holt, C.; Wittmann-Liebold, B., 1980: The primary structure of histone h 1 from sperm of the sea urchin parechinus angulosus 1. chemical and enzymatic fragmentation of the protein and the sequence of amino acids in the 4 amino terminal cyanogen bromide peptides. The primary structure of the amino-terminal 84 residues of sperm histone H1Parechinus was determined and presented.

Strickland W.N.; Strickland M.S.; D.G.oot P.C.; Von Holt C., 1980: Primary structure of histone h 2a from the sperm cell of the sea urchin parechinus angulosus. The 125 residues of the histone H2A from the sperm cells of the sea urchin P. angulosus were positioned. The N terminus is blocked by an acetyl group. Compared to the bovine histone, the sea urchin protein differs in 14 positions.

Strickland, W.N.; Strickland, M.S.; de Groot, P.C.; von Holt, C., 1980: The primary structure of histone H2A from the sperm cell of the sea urchin Parechinus angulosus. The 125 residues of the histone H2A from the sperm cells of the sea urchin Parechinus angulosus have been positioned. The N terminus is blocked by an acetyl group. Compared to the bovine histone, the sea urchin protein differs in 14 positions.

Strickland, WN.; Brandt, W.; Strickland, M.; Morgan, M. von Holt, C., 1974: The partial primary structure of two new arginine-serine rich histones from sperm of the sea urchin (Parechinus angulosus). South African Journal of Science, 702: 58

Kristensen, T.; Wierzbicki, D.M.; Sottrup-Jensen, L., 1984: Primary structure of human alpha 2 macro globulin 4. primary structure of 2 large cyanogen bromide fragments located in the carboxyl terminal part and accounting for 337 residues/. The amino acid sequences were determined for 2 CNBr fragments of human .alpha.2-macroglobulin which, due to the presence of an uncleaved Hse-Thr bond, form an MW = 40,000 fragment. These fragments are located in the COOH-terminal part of .alpha.2-...

Anonymous, 1975: Studies on the structure of rabbit muscle aldolase ec 41213 determination of the primary structure of the carboxy terminal cyanogen bromide peptide the complete sequence of the subunit poly peptide chain

Strickland, M.; Strickland, W.N.; Brandt, W.F.; Von Holt, C., 1977: The complete amino-acid sequence of histone H2B(1) from sperm of the sea urchin Parechinus angulosus. European Journal of Biochemistry 77(2): 263-275

Strickland, M.; Strickland, W.N.; Brandt, W.F.; Von Holt, C.; Wittmann-Liebold, B., 1978: The complete amino-acid sequence of histone H2B(3) from sperm of the sea urchin Parechinus angulosus. The primary structure of a third H2B histone isolated from sperm of the sea urchin Parechinus angulosus has been determined. H2B(3) consists of a polypeptide chain of the following 148 amino acid residues: Pro-Arg-Ser-Pro-Ala-Lys-Thr-Ser-Pro-Arg-L...