On the Hydrazinolysis of Proteins and Peptides: A Method for the Characterization of Carboxyl-terminal Amino Acids in Proteins

Akabori, Shirô; Ohno, Ko; Narita, Kozo

doi:10.1246/bcsj.25.214

Cited by 384 publications

(61 citation statements)

References 5 publications

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“…PTH-Arg and PTH-His were identified on an isocratic HPLC system on Partisil-5-PAC (Whatman; Suter, F. unpublished). Determination of the carboxy-terminal amino acid residue was achieved by hydrazinolysis as described in [13]. In order to determine the carboxy-terminal sequence, cleavage at aspartic acid [14] and at tryptophan [15] was performed.…”

Section: Methodsmentioning

confidence: 99%

The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

et al. 1987

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The bacteriochlorophyll a-binding polypeptide B80&866-8 was extracted from membranes of the green thermophilic bacterium ChloroJexus aurantiacus with chloroform/methanol/ammonium acetate. Purification of the antenna polypeptide (6.3 kDa) was achieved by chromatography on Sephadex LH-60, Whatman DE-32 and by FPLC. The complete amino acid sequence (53 amino acid residues) was determined. The B806-866-p polypeptide is sequence homologous to the antenna B-polypeptides of purple bacteria (27-40s) and exhibits the characteristic three domain structure of the B870, B80&850 and BSOO-820 antenna complexes. The two typical His residues, conserved in all antenna /?-polypeptides of purple bacteria, were found: His-24 lies within the N-terminal hydrophilic domain and His-42 within the central hydrophobic domain. This polypeptide together with the previously described a-polypeptide form the basic structural unit of the B806-866 antenna complex from C. aurantiacus.Green photosynthetic bacterium; B806-866 antenna complex; Light-harvesting polypeptide; Amino acid sequence;(Chlorojexus auran tiacus)

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Section: Methodsmentioning

confidence: 99%

The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

et al. 1987

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“…Amino-acid sequences of peptides were determined as described previously Hydrazinolysis was carried out by the method of Akabori et al [16] modified by Dautrevaux et al [17]. The COOH-terminal amino acid was identified by high-voltage paper electrophoresis at pH 3.0 (pyridine-acetic acid-water 3 : 120: 3877, v/v/v) followed by paper chromatography in solvent system butanol-acetic acid-water …”

Section: Methodsmentioning

confidence: 99%

Covalent Structure of Calf‐Thymus ALK‐Histone

Sautielère

Tyrou

Lainé

et al. 1974

European Journal of Biochemistry

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Highly purified calf thymus ALK-histone (histone rich in alanine, leucine and lysine) was isolated from Fza2 histone fraction by ion-exchange chromatography on Biorex 70 followed by gel filtration chromatography on Sephadex G-100. Peptides obtained by enzymatic hydrolyses (trypsin, chymotrypsin, thermolysin) of native or maleylated protein were fractionated by ionexchange chromatography on Chromobeads P.Thermolysin peptides which account for 127 of the 129 residues of the protein provide overlaps of tryptic and chymotryptic peptides and led us to establish the complete amino-acid sequence of ALK-histone as follows: Ser1-Gly-Arg-Gly-Lys-Gln-Gly-Gly-Lys-Ala-10Arg-Ala-Lys-Ala-LysThr-Arg-Ser-Ser-Arg20-Ala-Gly-Leu-Gln-Phe-Pro-Val-Gly-Arg-Val3o-His -Arg-Leu-Leu-Arg-LysGly-Asn-Tyr-Ala40-Glu-Arg-Val-Gly-Ala-Gly -Ma-Pro -Val-Tyr60-Leu -Ala-Ala-Val-Leu-Glu-TyrLeu-Thr-Ala~~-Glu-Ile-Leu-Gl~-Leu-Ala-Gly-Asn-Ala-Ala~~-Arg-Asp-Asn-Lys-Lys-Thr-Arg -IleIle-Proso-Arg-His-Leu-Gln-Leu-Ala-Ile-Arg-Asn-Aspso-Glu -Glu-Leu-Asn-Lys-Leu-Leu-Gly-LysVa1~~~-Thr-Ile-Ala-Gln-Gly-Gly-Val-Leu-Pro-Asn11o-Ile-Gln-Ala-Val-Leu-Leu-Pro-Lys-Lys-Thr~~~Glu-Ser-His-His-Lys-Ala-Lys-Gly-Lyslas.The amino end is acetylated. The sequence of ALK-histone is characterized by two hydrophobic regions, the first from Val-43 to Ala-70 and the second from Val-100 to Pro-117 and presents many repetitive or analogous sequences.The NH,-terminal sequence of ALK-histone is highly basic and shows a remarkable analogy with that of GRK-histone.A cluster of five basic residues His-His-Lys-Ala-Lys-Gly-Lys is present a t the COOH-terminal end.In the last five years refined methodology, combining selective and chromatographic or electrophoretic fractionation, has been set up for the separation of histones and has led to the isolation and Abbreviations. Dansyl, 5-dimethyl amino naphthalene-1-sulfonyl ; NMR, nuclear magnetic resonance.Nomenclature. The three-letter code used for the designation of histones emphasizes the three most abundant amino acids present in their molecule. GRK-histone = glycine, arginine, lysine-rich histone (formerly Fza1, histone IV or GAR-histone); KAS-histone = lysine, alanine, serine-rich histone (formerly Fzb, IIbz or LS-histone;) ARE-histone = alanine, arginine, glutamic acid-rich histone (formerly F, or histone 111) ; KAP-histone = lysine, alanine, proline-rich histone (formerly F, or very lysine-rich histone); ALKhistone = alanine, leucine, lysine-rich histone (formerly definition of five types of histones present in the nucleus of the somatic cell of mammals.The complete amino-acid sequence of three histones isolated from calf thymus has been determined: GRK-histone [1,2], 4] and AREhistone [5]. The primary structure of the KAPhistone from rabbit thymus is partially elucidated [61-A preliminary account of the complete aminoacid sequence of ALK-histone has already been reported [7]. Determination of the covalent structure of ALK-histone was initiated by an investigation of the tryptic and chymotryptic peptides from the native and maleylated protein...

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“…Substitution of this equation into the previous one gives the relationship n-h(vb-va)/VbP. This method has been used to perform replicate analyses on protein samples degraded with hydrazine by the method of Akabori et al 2 to determine the C-terminal residue. The resulting free C-terminal amino acid was separated from accompanying hydrazides by reaction of the latter with benzaldehyde.…”

Section: Resultsmentioning

confidence: 99%

Automatic Amino Acid Analysis of Replicate Samples

Stefanye¹,

Spero²

1963

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On the Hydrazinolysis of Proteins and Peptides: A Method for the Characterization of Carboxyl-terminal Amino Acids in Proteins

Cited by 384 publications

References 5 publications

The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

Covalent Structure of Calf‐Thymus ALK‐Histone

Automatic Amino Acid Analysis of Replicate Samples

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