Über ϵ-Markierung von Peptiden. Automatische Sequenzanalyse des Insulins

“…Factor IX and the light chains of factor X and protein C were sequenced in the automatic sequencer with mass spectrometric identification at positions Factor IX was degraded after modification with Braunitzer reagent III [21] in order to avoid contraction of the protein film in the spinning cup of the sequenator which otherwise occurred during evacuation with this protein from the first cycle. Despite these efforts no more than fourteen residues could be identified in factor IX.…”

Section: Resultsmentioning

confidence: 99%

Identification of γ‐carboxyglutamic acid residues in bovine factors IX and X, and in a new vitamin K‐dependent protein

Bucher¹,

Nebelin²,

Thomsen³

et al. 1976

FEBS Letters

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“…In common with calf thymus H2B [5,25] the amino-terminal region is highly basic. However, in H2B(1, of sea urchin the amino-terminal region shows an extension of 19 amino acids beyond the amino-terminal proline residue of calf H2B.…”

Section: Discussionmentioning

confidence: 99%

“…When lysine residues occurred at the carboxyl end of such a peptide the sequence analysis was further extended by coupling €-amino groups of lysine to 4-sulfophenylisothiocyanate [25]. Repetitive yields distinctly increased after modification of both carboxyl and &-amino groups.…”

Section: Discussionmentioning

confidence: 99%

“…In the first instance, 5.0 mg peptide were coupled with glycine methyl ester in the presence of l-ethyl-3-(dimethylamino-propy1)-carbodiimide [24]. In the second instance, 6.3 mg peptide were coupled as above and also 'anchored' into the cup by modification of the c-amino groups of lysine with 4-sulfophenylisothiocyanate [25]. If only the carboxyl groups were coupled Table 3.…”

Section: ---------------------------------------mentioning

confidence: 99%

See 1 more Smart Citation

The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus

Strickland

Brandt

et al. 1977

European Journal of Biochemistry

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Two histones have been isolated and purified from sperm cells of the sea urchin Parechinus angularus. They have been designated sperm histone H2B(1)1+,~~.~hi~~~ and sperm histone H2B~)~aveehinus on criteria of solubility and partial sequence homology with H2BCalf.H2B (1) consists of a polypeptide chain of the following 144 amino acid residues: Pro-Ser-GlnLys-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Gln-Lys-Gly Gly-Lys-Gly-Gly-Lys-Gly-Ala-Lys-Arg-Gly-Gly-Lys-Ala-Gly-Lys-Arg-Arg-Arg-Gly-Val-GlIn a previously published partial sequence serine was incorrectly assigned to position 30. A comparison of the carboxyl-terminal two thirds of H2B(1)parechinus and H2B,,lf reveals that 79 of the corresponding positions are occupied by identical amino acid residues. Much of the variability occurs in a short polar region of 20 amino acid residues. The remainder of C-terminal regions is hydrophobic and almost completely invariable.A comparison of the amino-terminal one third of H~B ( I ) P~~~,~~~~~~~ and H2B,,lc reveals that they are both highly basic with a considerable homology of the position of basic amino acids. Further, H2B(1)pavec,,inus possesses an amino terminal extension of 19 amino acids. These 19 amino acids can be recognized as a repeating pentapeptide.Five major species of histones have been recognized in calf thymus chromatin and their primary structures have been determined. These five histones have been described in other species as well and in a number of cases, the primary structures have been partially or completely determined. From these investigations it appears that the sequences of histones H3 and H4 are extremely conservative over a wide spectrum of the biological world [l], while that of HI is quite variable even between the HI histones isolated from different tissues of the same organism Ahhreviation. Dansyl, 5-dimethylaminonaphthalonesulfonyl. [2,3]. Histones H2A and H2B appear to be intermediate in variability [4-81. We have previously extracted two proteins from sperm of the sea urchin ParechinuJ angulosus that we classified by solubility criteria as H2B [9]. Partial sequence of these two proteins indicated a close homogology to calf thymus H2B at the carboxyl end. The N-terminal sequences, however, of the two proteins not only differed considerably from each other but showed little homology to calf thymus histone H2B. Nevertheless, these two sea urchin proteins were sub-classified as H2B(1) and H2B(2, on the strength of their solubility criteria and C-terminal sequence homologies. In this paper the complete amino acid sequence of sea urchin sperm histone H2B(1) is described, while the following paper presents the complete amino acid sequence of sea urchin hist one H 2B ( 2 ) .

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Über ϵ-Markierung von Peptiden. Automatische Sequenzanalyse des Insulins

Cited by 28 publications

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The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

Identification of γ‐carboxyglutamic acid residues in bovine factors IX and X, and in a new vitamin K‐dependent protein

The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus

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Über ϵ-Markierung von Peptiden. Automatische Sequenzanalyse des Insulins

Cited by 28 publications

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The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

Identification of γ‐carboxyglutamic acid residues in bovine factors IX and X, and in a new vitamin K‐dependent protein

The Complete Amino‐Acid Sequence of Histone H2B(1) from Sperm of the Sea Urchin Parechinus angulosus

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The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus