Search PubMed⌕ Search

Biomedical subjects

H Matsubara

Publications and source records attributed to H Matsubara.

At least 361 records · Page 20Linked to original sources
PubMed1985

Dissociation of bovine cytochrome c1 subcomplex and the status of cysteine residues in the subunits.

Purified bovine heart two-band cytochrome c1 subcomplex was dissociated by treatment with p-chloromercuribenzoic acid (pCMB) into its heme subunit and a colorless subunit called hinge protein, which is essential for the formation of cytochrome c1-c complex. The subcomplex was found by titration to react with 4 mol of pCMB per mol of cytochrome c1. The contents of mercury of the dissociated heme subunit and the hinge protein were 3 and 1 mol per mol of polypeptide, respectively. These results, together with the sequence analysis, indicated that the three cysteine residues in cytochrome c1 heme subunit not involved in heme-binding existed in free thiol form. One of the five cysteine residues in the hinge protein was in free form and four in two disulfide bonds. The dissociated hinge protein was digested with staphylococcal protease and the cysteine-containing peptides were separated by reversed-phase high-performance liquid chromatography (HPLC). The content of mercury and the result of performic acid oxidation of cystine peptides revealed that Cys-30 existed in free thiol form and two disulfide bridges were formed between Cys-24 and Cys-68 and between Cys-40 and Cys-54. The conformation of the hinge protein was predicted to be composed largely of either two-alpha-helical or four-alpha-helical conformation with the amino (N)-terminal 20 residues being in a random structure.

Amino Acid Sequence↗
PubMed1985

Effects of aldose reductase inhibitor on retinal microangiopathy in streptozotocin-diabetic rats.

Wistar strain rats were made diabetic by injection of streptozotocin and divided into three groups fed on different diets: conventional solid foods, a fructose-rich diet and a fructose-rich diet mixed with ONO 2235, an aldose reductase inhibitor. The retinas of these rats were examined in flat mount preparations after trypsinization. Microvascular changes such as capillary tortuosity, microaneurysms, pericyte loss, that are typical of diabetic retinal microangiopathy, were seen most frequently in the rats fed on the fructose-rich diet. The rats fed on the fructose-rich diet with ONO 2235 showed much less vascular change than the diabetic rats fed on the conventional food. Electron microscopy of the retina revealed localized thickening of the basement membrane of the retinal capillaries, and this was most frequent in the fructose-fed rats. However, in rats fed on fructose with ONO 2235 the changes of the basement membrane were slight. It was concluded that the aldose reductase inhibitor, ONO 2235, prevented development of diabetic microangiopathy, probably by suppressing the enzymatic activation of aldose reductase in the retina.

Aldehyde Reductase↗
PubMed1984

Complete amino-acid sequences of two isocytochromes c of the housefly, Musca domestica L., and their developmental variation in different tissues.

The complete amino-acid sequences of two isocytochromes c (larval- and adult-type cytochromes c) purified from the housefly Musca domestica L. were determined. Their sequences differed at six positions from each other. More than 90% of the total cytochrome c was larval-type during larval stages. The amount of adult-type cytochrome c increased rapidly from 1 day before adult emergence, making the total cytochrome c content increase to approximately 2.5-times as much cytochrome c content as in larvae. Although the major cytochrome c species in flight muscles was adult-type, imaginal disks contained mainly larval-type cytochrome c.

Amino Acid Sequence↗
PubMed1984

Structural homologies between the amino acid sequence of Clostridium pasteurianum MoFe protein and the DNA sequences of nifD and K genes of phylogenetically diverse bacteria.

The complete amino acid sequence of the larger (alpha-) subunit and about 70% of the total sequence of the smaller (beta-) subunit of the MoFe protein from Clostridium pasteurianum was determined by analyses of peptides derived from BrCN cleavage and by digestions with trypsin, staphylococcal protease and lysylendo-peptidase of the separated subunits. The alpha-subunit has 529 amino acid residues, giving an Mr value of 58 774. This is the first complete sequence for the alpha-subunit of an isolated MoFe protein. In comparing the sequences of both subunits to those from other sources, 5 out of 9 cysteines in the alpha-subunit and 3 out of 6 in the beta-subunit are invariant, thus suggesting a function as ligands to FeS and MoFeS clusters in the MoFe protein. All of these cysteines are located in the amino terminal halves of both subunits.

Amino Acid Sequence↗
PubMed1984

Juvenile nasal angiofibroma: a case report.

A very rare case of juvenile angiofibroma arising from the nasal septum is reported. To the best of our knowledge, this is the first such case reported in the literature. This tumour was ablated with surgical manipulation and electrocauterization. The pertinent literature is reviewed.

Adolescent↗
PubMed1984

Spirulina ferredoxin-NADP+ reductase. The complete amino acid sequence.

The amino acid sequence of ferredoxin-NADP+ oxidoreductase [EC 1.18.1.2, FNR] from Spirulina sp., a blue-green alga, was determined. Spirulina ferredoxin-NADP+ oxidoreductase was composed of 294 amino acid residues and the molecular weight of the holoenzyme was 34,135. An apparent homology of the amino(N)-terminal region was found between ferredoxin-NADP+ reductases from Spirulina and spinach. We also found some sequence similarities in human erythrocyte glutathione reductase and p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, both of which are NADPH-dependent FAD enzymes.

Amino Acid Sequence↗
PubMed1984

Ferredoxins from the photosynthetic purple non-sulfur bacterium Rhodopseudomonas palustris. Isolation and amino acid sequence of ferredoxin I.

Two ferredoxins, ferredoxins I and II, were prepared from Rhodopseudomonas palustris. They were separated on a Sephadex column after carboxymethylation and ferredoxin I, the major component, was subjected to an amino acid sequence study. The protein was composed of 63 amino acid residues and the sequence was as follows: (sequence; see text). The molecular weight was calculated to be 6,718, excluding iron and sulfur atoms. The distribution of the nine cysteine residues was similar to but clearly distinct from those of ferredoxins of other photosynthetic bacteria. Comparison of this ferredoxin with those of other bacteria suggests that the photosynthetic bacteria evolved on separate lines. Ferredoxin II was also subjected to analyses of amino acid composition and terminal sequences, but no further study was possible due to the limited material. Although the composition was different from that of ferredoxin I, the terminal sequences were exactly the same as those of ferredoxin I.

Amino Acid Sequence↗
PubMed1984

Serratia protease. Amino acid sequences of both termini, the 53 residues in the middle region containing the sole methionine residue, and a probable zinc-binding region.

Reexamination of the molecular mass and the amino acid composition of Serratia protease revealed the presence of 1 mol of methionine per mol of protein (about 46K daltons), and this was confirmed by BrCN cleavage followed by separation of the two fragments. The sole methionine residue was located near the middle region of the molecule. The amino(N)-terminal sequence was determined by Edman degradation of the protein and studies of several proteolytic peptides, establishing a sequence of 18 residues with a heterogeneous N-terminus. The carboxyl(C)-terminal sequence was determined by carboxypeptidase A digestion and tritium-labeling of the citraconylated C-terminal half segment to be -Phe-Ile-Val. The sequences of a total of 53 residues containing the methionine residue and a total of 38 residues containing two histidine residues were established by the application of various conventional methods to a BrCN peptide and several proteolytic peptides. The segment containing the histidine residues was homologous with that containing the two histidine residues chelating the zinc atom of thermolysin. The 38-residue segment may be directly connected to the 53-residue segment.

Amino Acid Sequence↗