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Biomedical subjects

T Hase

Publications and source records attributed to T Hase.

At least 217 records · Page 12Linked to original sources
PubMed1981

Correspondence of the larger subunit of the MoFe-protein in clostridial nitrogenase to the nif D gene products of other N2-fixing organisms.

The amino(N)-terminal sequence of the larger subunit (alpha) of the MoFe-protein from Clostridium pasteurianum was determined up to 179 amino acid residues by analyses of BrCN and tryptic peptides of the original subunit. Apparent similarities exist among the sequence of the clostridial alpha-subunit, that of the smaller subunit (beta) of the Azotobacter vinelandii MoFe protein, and those predicted from the nucleotide sequences of nif D genes in Klebsiella pneumoniae and Anabaena 7120. In comparing the sequences of C. pasteurianum and K. pneumoniae, 45% of residues are identical of a total of 184 sites. Therefore, the larger subunit of the clostridial MoFe-protein must correspond to the nif D gene product of K. pneumoniae.

Amino Acid Sequence↗
PubMed1981

Amino acid sequence of an intrinsic inhibitor of mitochondrial ATPase from yeast.

The amino acid sequence of an intrinsic inhibitor of mitochondrial ATPase isolated from yeast was completed by using solid-phase sequencing and conventional procedures. The inhibitor was found to be composed of 63 amino acid residues, to lack tryptophan, cysteine, and tyrosine, and to have a molecular weight of about 7,383. The inhibitor was characterized as a basic protein with 16 basic and 13 acidic amino acid residues, and several clusters of basic residues were noted. Some comments are made on the hydrophobic amino acids and the presence of repeated sequences.

Adenosine Triphosphatases↗
PubMed1981

Studies on algal cytochromes. III. Amino acid sequence of cytochrome c-553 from a brown alga, Petalonia fascia.

The amino acid sequence of a photosynthetic cytochrome c-553 isolated from a brown alga, Petalonia fascia was determined by BrCN fragmentation and a solid phase Edman degradation. The cytochrome contains 85 amino acid residues, giving a molecular weight of 9,803. The complete amino acid sequence is as follows: Val-Asp-Ile-Asn-Asn-Gly-Glu-Ser-Val-Phe-Thr-Ala-Asn-Cys-Ser-Ala-Cys-His-Ala-Gly -Gly-Asn-Asn-Val-Ile-Met-Pro-Glu-Lys-Thr-Leu-Lys-Lys-Asp-Ala-Leu-Glu-Glu-Asn-Gl u-Met-Asn-Asn-Ile-Lys-Ser-Ile-Thr-Tyr-Gln-Val-Thr-Asn-Gly-Lys-Asn-Ala-Met-Pro-A la-Phe-Gly-Gly-Arg-Leu-Ser-Glu-Thr-Asp-Ile-Glu-Asp-Val-Ala-Asn-Phe-Val-Ile-Ser-Gln-Ser-Gln-Lys-Gly-Trp. The highest homology was found between the sequences of cytochromes c-553 of P. fascia and Alaria esculenta, the next between those of P. fascia and Porphyria tenera.

Amino Acid Sequence↗
PubMed1981

The complete amino acid sequence of parsley (Petroserinum sativum) ferrodoxin.

The amino acid sequence of a ferredoxin from parsley (Petroserinum sativum) was determined by various conventional methods. Five tryptic peptides of carboxymethylated(Cm)-ferrodoxin were sequenced by a combination of automatic solid-phase and manual Edman degradations. The amino(N)-terminal sequences of Cm-ferrodoxin and its carboxy(C)-terminal half produced by tryptic cleavage specifically at the sole arginine residue of the molecule overlapped the five tryptic peptides. The molecule consists of 96 amino acid residues, including 5 cysteines, and lacks tryptophan. Parsley ferredoxin shows the greatest homology to wheat ferredoxin among other green plant ferredoxins.

Amino Acid Sequence↗
PubMed1981

X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 A resolution.

A [2Fe-2S] ferrodoxin from Spirulina platensis crystallized in space group C2221 with cell dimensions of a = 62.32, b = 28.51, c = 108.08 A, and alpha = beta = gamma = 90.0 degrees. X-ray structure analysis of the protein was carried out at 2.5 A resolution by the single isomorphous replacement method coupled with the derivative and the native anomalous dispersion methods. Phase angles of 2182 independent reflections were determined and their average figure of merit was 0.58. Each of 98 residues was superposed on the electron density sections enlarged to 2 cm/l A with a half-mirror device (Richards box). About 25% of the total residues form beta-structure and 10% fold in a tow-turn alpha-helix. A beta-barrel-like structure was found in the main chain fold. A polypeptide segment from residues 41 to 49 forms a loop structure outside the barrel. Two iron atoms of the [2Fe-2S] cluster are coordinated by three cysteines in the loop and by Cys-79. Hydrogen bonds of NH....S and OH....S stabilize the loop conformation. Most side chains are reasonably oriented in the molecule. The internal volume of the barrel is occupied by aliphatic nonpolar residues. All the charged groups are accessible to solvent molecules.

Binding Sites↗
PubMed1981

The second ferredoxin from spinach leaves.

A minor component of ferredoxin (about 20% of the total content) was separated from the major one on a DEAE Trisacryl M column only after carboxymethylation of the ferredoxin purified from spinach leaves by the conventional procedure. The amino acid compositions and terminal sequences of the two revealed that the major component corresponded to the one previously sequenced (Matsubara, H. & Sasaki, M. (1968) J. Biol. Chem. 243, 1732-1757) and the minor one had a completely different structure from that of the major one. Comparison of the amino(N)-terminal 34 residues showed 11 amino acid substitutions between the two components. Thus the existence of a second ferredoxin was demonstrated in spinach leaves.

Amino Acid Sequence↗
PubMed1980

Amino acid sequence of 2Fe-2S ferredoxin from an extreme halophile, Halobacterium of the Dead Sea.

The primary structure of the 2Fe-2S ferredoxin from Halobacterium of the Dead Sea was determined and it consisted of 128 amino acid residues including an N epsilon-acetyllysyl residue. Due to a high degree of sequence homology between this ferredoxin and the one from Halobacterium halobium, all tryptic peptides could be aligned in order. Only 20 amino acid differences were observed between these two halobacterial ferredoxins. The distribution of cysteinyl residues involved in the iron chelation was similar to that of chloroplast-type ferredoxins.

Amino Acid Sequence↗
PubMed1980

Amino acid sequence of a peptide containing an essential cysteine residue of yeast saccharopine dehydrogenase (L-lysine-forming).

The yeast saccharopine dehydrogenase (L-lysine-forming) contains an essential cysteine residue at the active site which can be carboxymethylated selectively by iodoacetate (Ogawa, H., Okamoto, M. and Fujioka, M. (1979) J. Biol. Chem. 254, 7030--7035). An undecapeptide containing this residue was isolated from the chymotryptic digest of the carboxymethylated enzyme by gel filtration chromatography and preparative paper electrophoresis. The amino acid sequence of the peptide was determined as Gly-Arg-Cys*-Gly-Ser-Gly-Ala-Leu-Ile-Asp-Leu, by the sequential Edman degradation and digestion with carboxypeptidases.

Amino Acid Sequence↗
PubMed1980

Amino acid sequences of two ferredoxins from Phytolacca esculenta. Gene duplication and speciation .

The amino acid sequences of two ferredoxins from Phytolacca esculenta were determined by a combination of solid-phase sequencing and the conventional methods. Ferredoxins I and II were composed of 96 and 98 amino acid residues, respectively, and ferredoxin I showed sequence heterogeneity at two positions. The amino acid sequences of ferredoxins I and II from Phytolacca esculenta were very similar to those of corresponding ferredoxins I and II from Phytolacca americana. Amino acid differences among Phytolacca ferredoxins and other higher plant ferredoxins suggest that duplication of the ferredoxin gene occurred after the divergence of Phytolacca from other higher plants and preceded the separation of two species of Phytolacca.

Amino Acid Sequence↗
PubMed1980

Amino acid sequence of a purothionin homolog from barley flour.

A purothionin homolog was isolated from barley flour and purified by CM-52 column chromatography. It showed potent lethal activity towards brewer's yeast and its complete amino acid sequence was determined to be as follows. Lys-Ser-Cys-Cys-Arg-Ser-Thr-Leu-Gly-Arg-Asn-Cys-Tyr-Asn-Leu-Cys-Arg-Val-Arg-Gly-Ala-Gln-Lys-Leu-Cys-Ala-Gly-Val-Cys-Arg-Cys-Lys-Leu-Thr-Ser-Ser-Gly-Lys-Cys-Pro-Thr-Gly-Phe-Pro-Lys. It thus consists of 45 amino acid residues with 8 cysteines. The number of amino acid residues and the positions of the 8 cysteines are identical with those of wheat purothionins. There is a high degree of homology in the primary structures of these proteins.

Amino Acid Sequence↗
PubMed1980

Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris, Miyazaki.

The complete amino acid sequence of a tetrahemoprotein, cytochrome c3 isolated from Desulfovibrio vulgaris, Miyazaki, was determined to be Ala-Pro-Lys-Ala-Pro-Ala-Asp-Gly-Leu-Lys-Met-Asp-Lys-Thr-Lys-Gln-Pro-Val-Val-Phe -Asn-His-Ser-Thr-His-Lys-Ala-Val-Lys-Cys-Gly-Asp-Cys-His-His-Pro-Val-Asn-Gly-Lys-Glu-Asn-Tyr-Gln-Lys-Cys-Ala-Thr-Ala-Gly-Cys-His-Asp-Asn-Met-Asp-Lys-Lys-Asp-Lys-Ser-Ala-Lys-Gly-Tyr-Tyr-His-Ala-Met-His-Asp-Lys-Gly-Thr-Lys-Phe-Lys-Ser-Cys-Val-Gly-Cys-His-Leu-Glu-Thr-Ala-Gly-Ala-Asp-Ala-Ala-Lys-Lys-Lys-Glu-Leu-Thr-Gly-Cys-Lys-Gly-Ser-Lys-Cys-His-Ser. The highest homology was found between the sequence of cytochrome c3 of D. vulgaris, Miyazaki, and that of D. vulgaris, Hildenborough, on comparison among various cytochrome c3'S. These two consist of 107 amino acid residues and they differ by 14 residues.

Amino Acid Sequence↗
PubMed1979

Structural and evolution of chloroplast- and bacterial-type ferredoxins.

Comparisons have been made between amino acid sequences of 26 chloroplast-type ferredoxins and 16 bacterial-type ferredoxins. Their structural characteristics are described and related to a three-dimensional structure of a chloroplast-type ferredoxin. Aspects of molecular evolution of these ferredoxins are presented together with a phylogenetic tree including both chloroplast- and bacterial-type ferredoxins.

Amino Acid Sequence↗
PubMed1978

Amino acid sequence around the pyridoxal 5'-phosphate binding site in potato phosphorylase.

The amino acid sequence around the pyridoxal 5'-phosphate binding site in potato phosphorylase was determined in order to compare it with those in phosphorylases from other sources having different regulatory properties. The potato enzyme was reduced by NaBH4 in the presence of urea, carboxymethylated, and digested with chymotrypsin and trypsin. Pyridoxyl peptides were isolated by the differential procedure using paper electrophoresis or DEAE-cellulose column chromatography. In Edman degradation of these peptides, pyridoxyllysine was identified as the phenylthiohydantoin derivative of pyridoxyllysine using a combination of thin-layer chromatography and the Pauli reaction. The sequence around pyridoxyllysine, comprising 57 amino acid residues, was determined except for a region with 6 amino acid residues. The pyridoxal 5'-phosphate binding site in potato phosphorylase showed a high homology with those of the rabbit muscle and yeast enzymes. This finding suggests that the cofactor should be directly related to the essential process of phosphorylase action.

Amino Acid Sequence↗
PubMed1978

Amino acid sequences of two ferredoxins from pokeweed, Phytolacca americana.

The amino acid sequences of two ferredoxins isolated from pokeweed, Phytolacca americana, were determined. Tryptic peptides of maleyl-carboxymethyl-ferredoxin I and carboxymethyl-ferredoxin II were prepared and analyzed. The large peptides were further digested with staphylococcal protease and chymotrypsin. Ferredoxins I and II were composed of 96 and 98 amino acid residues, respectively. Though ferredoxin I lacks tryptophan and methionine, ferredoxin II contains both of them. In a comparison of the amino acid sequences with those of other higher plant ferredoxins, ferredoxin I is one residue shorter than others at the carboxyl-terminus and ferredoxin II one longer than others at the amino-terminus. Ferredoxins I and II differ in 23 sites from each other and in 27 to 37 sites from other higher plant ferredoxins. This suggests that duplication of the ferredoxin gene occurred after the divergence of pokeweed from other higher plants. A phylogenetic tree including all other ferredoxins was constructed.

Amino Acid Sequence↗