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M Haniu

Publications and source records attributed to M Haniu.

At least 73 records · Page 4Linked to original sources
PubMed1979

Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the heme alpha-containing subunit.

The complete amino acid sequence of the heme alpha-containing subunit V of bovine heart cytochrome oxidase was determined to be: H2N-Ser-His-Gly-Ser-His-Glu-Thr-Asp-Glu-Glu-Phe-Asp-Ala-Arg-Trp-Val-Thr-Tyr-Phe-Asn-Lys-Pro-Asp-Ile-Asp-Ala-Trp-Glu-Leu-Arg-Lys-Gly-Met-Asn-Thr-Leu-Val-Gly-Tyr-Asp-Leu-Val-Pro-Glu-Pro-Lys-Ile-Ile-Asp-Ala-Ala-Leu-Arg-Ala-Cys-Arg-Arg-Leu-Asn-Asp-Phe-Ala-Ser-Ala-Val-Arg-Ile-Leu-Glu-Val-Val-Lys-Asp-Lys-Ala-Gly-Pro-His-Lys-Glu-Ile-Tyr-Pro-Tyr-Val-Ile-Gln-Glu-Leu-Arg-Pro-Thr-Leu-Asn-Glu-Leu-Gly-Ile-Ser-Thr-Pro-Glu-Glu-Leu-Gly-Leu-Asp-Lys-Val-COOH. The subunit V is a single polypeptide which consists of 109 amino acid residues. The protein contains 48.6% hydrophobic residues and 34.0% hydrophilic residues and it is an acidic protein having a net charge of -3 at neutral pH. The molecular weight of subunit V was calculated to be 12,436 and that for the heme alpha-containing polypeptide was 13,295.

Amino Acid Sequence↗
PubMed1977

The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides.

A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein (N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis, carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2) accounted for the 273 amino acid residues present in the iron protein.

Amino Acid Sequence↗
PubMed1977

The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. II. Cyanogen bromide peptides.

A total of 10 cyanogen bromide peptides were isolated from the S-beta-carboxymethyl iron protein of nitrogenase. Purification of these peptides was performed mainly by gel filtration on Sephadex G-50; by ascending paper chromatography using the solvent system of pyridine, isoamyl alcohol, 0.1 M ammonium hydroxide; and also, in some cases, with additional steps such as anion exchange column chromatography on Dowex 1-X2 or ascending paper chromatography in an acidic solvent system or by pyridine precipitation of the cyanogen bromide fragment. Sequenator analyses of three large cyanogen bromide peptides (53 to 72 residues) provided tryptic peptide overlap data for the inner portion of the protein. The cyanogen bromide peptides accounted for all of the 273 amino acid residues which were present in the tryptic peptides isolated from carboxymethyl-iron protein (Tanaka, M., Haniu, M., Yasunobu, K. T., and Mortenson, L. E. (1977) J. Biol. Chem. 252, 7081-7088).

Amino Acid Sequence↗
PubMed1975

Modification of the automated sequence determination as applied to the sequence determination of the Spirulina maxima ferredoxin.

The amino acid sequence of the Spirulina maxima ferredoxin was shown to be: H2N-Ala-Thr-Tyr-Lys-Val-Thr-Leu-Ile-Ser-Glu-Ala-Glu-Gly-Ile-Asn-Glu-Thr-Ile-Asp-Cys-Asp-Asp-Asp-Thr-Tyr-Ile-Leu-Asp-Ala-Ala-Glu-Glu-Ala-Gly-Leu-Asp-Leu-Pro-Tyr-Ser-Cys-Arg-Ala-Gly-Ala-Cys-Ser-Thr-Cys-Ala-Gly-Lys-Ile-Thr-Ser-Gly-Ser-Ile-Asp-Gln-Ser-Asp-Gln-Ser-Phe-Leu-Asp-Asp-asp-Gln-Ile-Gln-Ala-Gly-Tyr-Val-Leu-Thr-Cys-Val-Ala-Tyr-Pro-Thr-Ser-Asp-Cys-Thr-Ile-Gln-Thr-His-Gln-Glu-Glu-Gly-Leu-Tyr-COOH. The S. maxima ferredoxin is the first procaryote ferredoxin of the plant-algal type to be reported. A modification of the automated sequence determination of a peptide, which was extracted by the organic solvents used to remove excess reagents and the amino acid thiazoline, was utilized to complete the sequence of a 36 residue tryptic peptide.

Amino Acid Sequence↗
PubMed1975

The amino acid sequence of ferredoxin II from Chlorobium limicola, a photosynthetic green bacterium.

The amino acid sequence of ferredoxin II from the photosynthetic green sulfur-reducing bacterium, Chlorobium limicola, was deduced to be: Ala-His-Arg-Ile-Thr-Glu-Glu-Cys-Thr-Tyr-Cys-Ala-Ala-Cys-Glu-Pro-Glu-Cys-Pro-Val-Asn-Ala-Ile-Ser-Ala-Gly-Asp-Glu-Ile-Tyr-Ile-Val-Asp-Glu-Ser-Val-Cys-Thr-Asp-Cys-Glu-Gly-Tyr-Tyr-Asp-Glu-Pro-Ala-Cys-Val-Ala-Val-Cys-Pro-Val-Asp-Cys-Ile-Ile-Lys-Val. The ferredoxin was shown to consist of 61 amino acids in a single polypeptide chain. The presence of 8 g-atoms of Fe and 8 mol of sulfide led to a calculated molecular weight of 7289. In constract to the ferredoxin I from C. limicola, ferredoxin II contains basic amino acids in positions 2 and 3 and 60 from the NH(2)-terminal end of the protein. The sequences of all the various ferredoxins from photosynthetic bacteria reported to date are compared with one another.

Amino Acid Sequence↗