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Biomedical subjects

H Matsubara

Publications and source records attributed to H Matsubara.

At least 433 records · Page 24Linked to original sources
PubMed1980

Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences.

To elucidate the structural similarity between alpha-glucan phosphorylases from different sources, the amino acid sequences of the cysteinyl regions in potato phosphorylase were determined, and compared with the complete sequence of the rabbit muscle enzyme. Cysteinyl peptides were purified by covalent chromatography based on thiol-disulfide exchange. Potato phosphorylase was coupled to Thiopropyl-Sepharose 6B in the presence of urea, and, after tryptic digestion, 10 distinct cysteinyl peptides which accounted for all the cysteine present in the enzyme were finally isolated in high yields. From the sequence comparison, all of the peptides surrounding the cysteinyl residues in the potato enzyme are homologous with widely distributed specific regions in the rabbit muscle enzyme, although only 4 of 10 cysteinyl residues are conserved between the two enzymes. These observations, in addition to the previously established homology in the cofactor site, show that potato and rabbit muscle phosphorylases are similar in terms of the primary structure. The different properties of cysteinyl residues in the two enzymes are discussed based on the present sequence comparison and the recent X-ray crystallographic data for the rabbit muscle enzyme.

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↗
PubMed1979

Isolation and characterization of two ferredoxin-NADP+ reductases from Spirulina platensis.

Two ferredoxin-NADP+ reductases (FNRs I and II) [EC 1.6.7.1] were purified from a blue-green alga, Spirulina platensis, by (NH4)2SO4 fractionation, gel filtration on Sephadex G-100 and DEAE-Sephadex A-50 chromatography. FNRs I and II were both FAD-containing enzymes with molecular weights of 33,000, and could photochemically reduce NADP+ to the same extent in the presence of S. platensis ferredoxin, using FNR-depleted membrane fragments of S. platensis. They had similar physical and enzymatic properties, except for chemical properties such as the amino (N)-terminal sequences and the patterns of their peptide maps. The significance of the presence of two FNRs in S. platensis as as of the multiple forms found in other organisms is discussed.

Amino Acid Sequence↗
PubMed1979

Physiological changes in the treatment of acrophobia (fear of height).

In order to investigate the physiological changes produced by the treatment of acrophobic patients body movement and Microvibration were measured before and after treatment. Eighteen acrophobic patients were assigned at random to 1 of the 2 groups: a treatment group (n = 8) and a non-treatment group (n = 10). The control group consisted of 16 healthy volunteers. Body movement area while viewing a slide of a high place or imagining a high place in the treatment group decreased significantly after treatment. Body movement of the control group showed almost no changes, and that of the non-treatment group was situated between the above-mentioned 2 groups. Simple body movements of the acrophobic patients without any stimulation of height were bigger than those of the control subjects. MV pattern of the treatment group had a tendency to improve under psycho-therapy. Acrophobic patients had more abnormal MV patterns than the normal subjects.

Adult↗
PubMed1979

Bilateral Meniere's disease.

A survey of 265 Japanese patients with Meniere's disease revealed bilateral involvement in approximately 29% of all these patients. Somatic and psychiatric aspects of bilateral Meniere's disease were as follows. (1) The duration of the disease in cases of bilateral involvement was significantly longer than cases of unilateral involvement. (2) An abnormal general condition, a more extensive degree of hearing loss and neurotic type were frequently diagnosed in cases of bilateral involvement. Based on these results, it was concluded that psychiatric management and prevention of aggravation of deafness should be part of the management of treatment in bilateral Meniere's disease.

Female↗
PubMed1978

Biofeedback modification of frontal EMG in normal subjects.

We carried out a controlled study on the voluntary control of the frontalis muscle by biofeedback procedures employing 20 normal subjects. Subjects were randomly divided into two groups of 10: (1) the biofeedback group and (2) the control group. Each of the two groups received five training sessions of about 40 minutes' duration each on different days. The results obtained are as follows: (1) In the biofeedback group, mean EMG levels decreased progressively and markedly from 2. 16 muVp-p min the first session to 1.54 muVp-p min in the last session. On the contrary, the control group did not show constant decreases in EMG levels over sessions. (2) The changes in the heart rate did not correlate with the changes in EMG activity. (3) The changes in the respiratory rate correlated with the changes in EMG activity.

Adult↗
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↗
PubMed1978

Amino acid sequence of a ferredoxin from Chlorobium thiosulfatophilum strain Tassajara, a photosynthetic green sulfur bacterium.

We have determined the amino acid sequence of a ferredoxin from a photosynthetic green sulfur bacterium, Chlorobium thiosulfatophilum strain Tassajara. It contains 61 amino acid residues with 9 cysteines, and 8 of the 9 were located at positions corresponding to those in clostridial-type ferredoxins. Other structural features were closer to those of ferredoxins from another photosynthetic bacterium, C. limicola, than to those of non-photosynthetic bacteria. Compared with ferredoxin from Chromatium, a photosynthetic purple sulfur bacterium, all photosynthetic bacterial ferredoxins have a common region in the carboxyl-terminal half with several extra residues and a unique cysteine residue. We compared all the photosynthetic bacterial ferredoxins that have been sequenced and concluded that C. thiosulfatophilum ferredoxin is most closely related to C. limicola ferredoxin I.

Amino Acid Sequence↗
PubMed1978

Complete amino acid sequence of Halobacterium halobium ferredoxin containing an Nepsilon-acetyllysine residue.

1. The complete amino acid sequence of the 2Fe-2S ferredoxin from Halobacterium halobium was determined to be: (formula see text):2. The apoferredoxin chain consists of 128 amino acid residues and has a molecular weight of 14,330. 3. There are only four cysteines in this ferredoxin molecule; they should be involved in the binding of the two iron atoms at the active center. Ther relative positions of these cysteines are similar to those of the cysteines in chloroplast ferredoxins. 4. There is a high degree of homology between H. halobium ferredoxin and chloroplast ferredoxins, though the latter molecules contain only about 98 amino acid residues. 5. H. halobium ferredoxin contains a single residue of Nepsilon-acetyllysine.

Amino Acid Sequence↗