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Biomedical subjects

K Narita

Publications and source records attributed to K Narita.

At least 19 recordsLinked to original sources
PubMed1992

The absorbance spectrum and photosensitivity of a new synthetic "visual pigment" based on 4-hydroxyretinal.

The firefly squid, Watasenia scintillans, is the only animal known to possess a visual pigment in which the chromophore is 4-hydroxyretinal. This paper describes the absorbance spectrum and some properties of a synthetic "A4" visual pigment generated from bovine opsin and 4-hydroxyretinal. The absorbance spectrum of this pigment is compared with (a) bovine rhodopsin and (b) a rhodopsin template with the same lambda max as the synthetic visual pigment. The A4 pigment is shown to have an absorbance spectrum that is almost identical to that of a rhodopsin template. It is also shown that the photosensitivity and thermal stability of the A4 pigment, dispersed in detergent micelles, is essentially similar to that of rhodopsin.

Animals↗
PubMed1992

[A case of hepatic hydrothorax treated by pleuro-venous shunt].

We reported a successful pleuro-venous shunt operation (Pl-V shunt) for a patient of liver cirrhosis with secondary hydrothorax. A 78-year-old female was admitted to our hospital because of severe dyspnea and palpitation. Chest x-ray film revealed right sided massive pleural effusion. Over several weeks the chest tube drainaged about 1,500 ml of transudative fluid per day. We performed Pl-V shunting and pleural effusion subsequently decreased in amount and dyspnea disappeared. This Pl-V shunting is thought to be useful for such a patient with massive pleural effusion which failed to respond to medical therapy.

Aged↗
PubMed1992

[A successfully treated case of empyema with a large tracheal fistula after a radical operation of esophageal cancer by fixation and plombage with major pectoral muscle flap].

We reported a successfully treated case of empyema with a large tracheal fistula which had developed after a radical operation of esophageal cancer (reconstructed with stomach). This 59-year-old male was treated by the method of fixation and plombage with major pectoral muscle flap and thoracoplasty, because we could not use the omentum that were frequently used nowadays for closure of the fistula. The size of the tracheal fistula was a large as the main bronchus bronchoscopically. Postoperative care were the following, the endotracheal tube was inserted from the tracheal stoma to the left main bronchus and 9 days left hemi-ventilation was performed. Continuous suction was performed at the same time from the right main bronchus in order to prevent secretion and blood pour into the left lung. Bronchoscopical examination done 28 postoperative day, the small fistula remained the tip of the muscle flap. But 72 postoperative day, the surface of the fixed muscle flap was replaced by normal bronchial mucomembrane and tracheal fistula was obliterated. Major pectoral muscle could be used as local flap to obliterate empyema cavity associated with tracheal fistula. We believe that utilizing an muscle flap for those who had undergone abdominal operation like our case is a valuable method.

Empyema↗
PubMed1979

Primary structure of the membrane-binding segment of rabbit cytochrome b5.

The primary structure of the membrane-binding segment of rabbit cytochrome b5 has been determined. This segment, prepared by trypsin digestion of the intact protein, consists of 43 amino acid residues and corresponds to the COOH-terminal end (residues 91-133) of the parent molecule. Deduction of the primary structure was based on automated sequence analysis of the whole segment as well as manual and dansyl-Edman degradations of peptide fragments produced by CNBr cleavage and partial acid hydrolysis. The sequence obtained is: Leu-Ser-Lys-Pro-Met-Glu-Thr-Leu-Ile-Thr-Thr-Val-Asn-Ser-Asn-Ser-Ser-Trp-Trp-Thr-Asn-Trp-Val-Ile-Pro-Ala-Ile-Ser-Ala-Leu-Ile-Val-Ala-Leu-Met-Tyr-Arg-Leu-Tyr-Met-Ala-Asp-Asp. This sequence is 63 to 81% homologous with respect to those determined for the membrane-binding segments of equine, porcine and bovine cytochrome b5. The interaction of this segment with phospholipid bilayer membranes is discussed, and a prediction of its secondary structure is also presented.

Amino Acid Sequence↗
PubMed1979

Hydrogen-tritium exchange titration of the histidine residues in bovine heart cytochrome c and analysis of their microenvironment.

Microenvironments of the three histidine residues located at the positions 18, 26, and 33 from the amino terminus in bovine heart cytochrome c were analysed in solution by the hydrogen-tritium exchange titration method, which has been developed in this laboratory. Histidine-18, which is liganded to the heme iron, and histidine-26 did not incorporate tritium in native state, indicating that the two are located in solvent inaccessible hydrophobic regions. Histidine-33 was labeled with tritium to an appreciable extent and seemed to be partially buried in the molecule. The pKa value estimated for histidine-33 was 6.1 at 37 degrees by the tritium exchange titration, suggesting that the residue interacts very weakly with a neighboring cationic group. These results seem to be compatible with the tertiary structure of the protein deduced from the X-ray crystallographic analysis.

Amino Acid Sequence↗
PubMed1978

Amino acid sequences of the two polypeptide chains in beta1-bungarotoxin from the venom of Bungarus multicinctus.

The two dissimilar composite polypeptide chains (A and B) in beta1-bungarotoxin were isolated as their reduced and carboxymethylated derivatives as reported in the preceding paper. The N-terminal sequences were determined with a sequenator up to the 39th residue for the RCM-A chain and up to the 25th residue for the RCM-B chain with repetitive yields of 90-95%. The tryptic and chymotryptic peptides from the two chains were isolated and their structures were determined by manual Edman degradation together with dansyl-Edman and carboxypeptidases A and Y. To complete the primary structures of the two chains, information on the tryptic peptides derived from the maleylated derivatives of the two chains was also used. The completed amino acid sequence of the A chain containing 120 residues (molecular weight, 13,500) is similar to that of notexin, a presynaptic neurotoxin from Australian tiger snake venom, and phospholipases A from other snake venoms. The amino acid sequence of the 60 residues in the B chain (molecular weight, 7,000) bears no resemblance to any basic polypeptides from snake venoms. The B chain probably plays a significant role by interacting with some components in presynaptic membranes of neurosmuscular junctions.

Amino Acid Sequence↗
PubMed1978

Chemical properties and amino acid composition of beta1-bungarotoxin from the venom of Bungarus multicinctus (Formosan banded krait).

beta-Bungarotoxin purified from the venom of Bungarus multicinctus (Formosan banded krait) contained no carbohydrate and behaved as a homogeneous protein on polyacrylamide gel electrophoresis at pH 4.1 and SDS-polyacrylamide gel electrophoresis without 2-mercaptoethanol treatment. Its molecular weight and isoelectric point were estimated to be about 21,000 by gel filtration and about 9.5 by isoelectric focusing, respectively. The toxin treated with the reducing agent was split into two polypeptide chains as revealed by SDS-polyacrylamide gel electrophoresis and their molecular weights were calculated to be about 13,000 and 7,000. The two polypeptide chains (the large one named the A chain and the small one the B chain) were isolated by gel filtration after reduction of disulfide bonds in the toxin followed by alkylation. The A chain contained 120 amino acid residues including 13 half-cystines and the B chain 60 residues including 7 half-cystines. The two chains were supposed to link by disulfide bond(s) in the intact toxin which contained no free sulfhydryl groups. The N-terminal residues of the A and B chains were asparagine and arginine and the C-terminal ones were glutamine and proline, respectively, in accordance with the results of the terminal analyses of the intact toxin.

Amino Acids↗
PubMed1978

Chemical modification of ribonuclease T1 with ozone.

The single tryptophan residue in ribonuclease T1 [EC 3.1.4.8] was selectively oxidized by ozone to N'-formylkynurenine, which was then converted to kynurenine by acid-catalyzed deformylation in the frozen state. The two enzyme derivatives thus formed, NFK- and Kyn-RNase T1, lost enzymatic activity at pH 7.5, at which native RNase T1 most efficiently catalyzes the hydrolysis of RNA. At pH 4.75, the modified enzymes retained a decreased but distinct enzymatic activity toward RNA without alteration of substrate specificity, and Kyn-RNase T1 was four times more active than NFK-RNase T1. The binding of 3'-GMP to these modified enzymes decreased remarkably at pH 5.5, the optimum pH for binding to the intact enzyme. The gamma-carboxyl group of glutamic acid 58 was still reactive to iodoacetic acid after modification of tryptophan 59. The amounts of the carboxymethyl group introduced into NFK- and Kyn-RNase T1 were 0.36 and 0.59 mol, respectively, under conditions such that quantitative esterification of native RNase T1 takes place. CD spectroscopy indicated that the tertiary structure of the molecule was disordered in NFK-RNase T1, but not significantly in Kyn-RNase T1. It is concluded that tryptophan 59 functions in maintaining the active conformation of the protein structure, particularly in constructing the active environment for a functionally important set of groups involved in the binding of the substrate at the active site, although direct participation of in tryptophan the catalytic function of ribonuclease T1 is unlikely.

Chemical Phenomena↗
PubMed1978

Characterization of phospholipase A activity of beta1-bungarotoxin from Bungarus multicinctus venom. II. Identification of the histidine residue of beta1-bungarotoxin modified by p-bromophenacyl bromide.

beta1-Bungarotoxin modified with p-bromophenacyl bromide (BPB) was reduced and carboxymethylated, and the resulting two constituent RCM-polypeptide chains (the RCM-A and B chains) were separated. The RCM-A chain was found to be modified by BPB by measuring its UV absorption spectrum and was shown to have lost one histidine residue by analyzing its amino acid composition. To determine the location of the modified histidine residue in the A chain of the toxin, the RCM-A chain was digested with TPCK-trypsin, and the resulting peptides were fractionated by gel filtration followed by DEAE-cellulose chromatography. The modified residue was finally identified as histidine-48 in the A chain by Edman degradation and from the amino acid composition of the BPB-modified peptide. The amino acid sequence around the modified histidine residue in the A chain is highly homologous with those of porcine pancreas phospholipase A2 and presynaptic toxin, notexin. We conclude that histidine-48 in the A chain participates in the phospholipase A activity of beta1-bungarotoxin.

Acetophenones↗
PubMed1978

Location of disulfide bridges in cardiotoxin from the venom of Formosan cobra (NAJA NAJA ATRA).

The location of the four disulfide bridges in cardiotoxin from the venom of the Formosan cobra, Naja naja atra, was determined by isolating cystine-containing peptides from the enzymic and partial acid hydrolyzates of the intact toxin. The results indicate that the disulfide bridges are formed by half cystine residues 3--21, 14--38, 42--53, and 54--59. The amino acid sequence at the position 48--49 was revised to -Leu-Val- instead of Val-Leu- as reported previously.

Amino Acid Sequence↗