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Biomedical subjects

K Wada

Publications and source records attributed to K Wada.

At least 775 records · Page 43Linked to original sources
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↗
PubMed1981

Experimental myocarditis. II. Cardiac lesions in rats induced by immunization with heterologous heart extracts.

The production of myocardial lesions and circulating anti-heart antibodies has been studied in the present experiment. Twenty-one of Wistar rats were divided into 3 groups: 9 rats immunized with heterologous heart extracts, Freund's complete adjuvant and diphtheria-tetanus-pertussis (DTP) vaccine, 8 rats injected phosphate buffered saline adjuvant mixture with DTP vaccine and 4 rats untreated as control. Injection of heterologous heart extracts emulsified with Freund's complete adjuvant and DTP vaccine developed focal myocardial lesions in all of the subjected rats. The lesions were characterized by focal and diffuse interstitial cellular infiltration with myocardial necrosis. The circulating antibodies reacted to rat heart extracts were detected in 77.8% of the subjects. The antigen, reacted with the antibodies, located intracellular spaces in myocardium. The severity of cardiac lesions were not functional to the titer of circulating anti-heart antibodies may play little role in the pathogenesis of myocardial damage at least in this experimental myocarditis.

Animals↗
PubMed1981

[Laboratory and clinical studies on ceftizoxime in otorhinolaryngological field (author's transl)].

From the laboratory and clinical studies on ceftizoxime (CZX), the following results were obtained 1) CZX was compared with cefazolin (CEZ) for in vitro activity against 6 standard strains and clinically isolated strains of Staphylococcus aureus (19 strains), Staphylococcus epidermidis (14), Proteus sp. (17), Escherichia coli (3), Klebsiella sp. (3) and Pseudomonas aeruginosa (13). While somewhat less active against Gram-positive cocci than CEZ, CZX was far more active than CEZ against Gram-negative bacilli. 2) The time course of mean serum CZX levels in 2 patients given a single intravenous dose of 10 mg/kg was as follows: 24.9 microgram/ml at 15 minutes, 18.5 microgram/ml at 30 minutes, 13.2 microgram/ml at 1 hour, 6.4 microgram/ml at 2 hours and 2.7 microgram/ml at 4 hours. The mean serum half life was 1.36 hours. The mean tonsil concentrations of CZX 30 minutes after a single intravenous dose of 0.5 g and 1.0 g were 5.9 microgram/g and 9.6 microgram/g. respectively, with the ratio to the serum concentration of 0.33 and 0.32. 3) CZX was given to 28 patients with ear, nose, and throat infections, and overall rate of effectiveness was 92.3%. No clinical side effects were observed. Changes in laboratory test findings included slightly elevated GOT and/or GPT in 3 cases.

Adolescent↗
PubMed1981

Increased activity of a neutral protease in cytosol from rat hepatoma induced by N-2-fluorenylacetamide.

A protease active with N-alpha-benzoyl-DL-arginine-p-nitroanilide with an optimum pH of 7.3 has been found in the cytosol of rat liver. The activity of this protease increased in N-2-fluorenylacetamide-induced hepatoma as well as in fetal liver. It has been purified from normal liver and hepatoma about 200-fold. Its molecular weight is estimated by gel filtration to be about 200,000 in each tissue. The protease activity is unaffected by chymostatin, pepstatin, soybean trypsin inhibitor, and p-chloromercuribenzoate. Antipain, leupeptin, tosyl-L-lysine chloromethyl ketone, and phenylmethylsulfonyl fluoride inhibit the protease activity. This protease appears to be a serine protease.

2-Acetylaminofluorene↗
PubMed1980

A protease from rat intestine.

Partially purified ribonuclease H from rat liver nuclei can be inactivated by a soluble fraction from rat intestine; this inactivation is restored by adding trypsin inhibitor, suggesting that the factor is a protease. A preparation has been isolated and purified to homogeneity. The molecular weight of the enzyme was estimated as 28 000 with an optimum pH of 8.0 and an isoelectric point at pH 4.5--4.7. The inactivating and proteolytic activities were observed in parallel throughout the purification procedures. Diisopropylphosphorofluoridate inhibited the protease activity. The protease inactivates deoxyribonuclease I, pyruvate kinase, and aldolase. From experiments with protease modifiers, it seems to be a serine protease of a trypsin-like nature.

Animals↗
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

Experimental myocarditis. I. Cardiac lesions in rats induced by immunization with homologous heart extracts.

The production of myocardial lesions and circulating anti-heart antibodies has been studied in rats injected with homologous heart extracts emulsified with the Freund's complete adjuvant and the DTP vaccine. Six of 7 rats showed lesions of focal myocarditis, while only in one of them circulating anti-heart antibodies were detected. There was no correlation between the presence of circulating anti-heart antibodies and that of myocardial lesions. These findings suggested that the circulating anti-heart antibodies may play little or no role in the pathogenesis of this experimental myocarditis.

Animals↗
PubMed1980

Acetylcholine receptor in rabbit thymus: antigenic similarity between acetylcholine receptors of muscle and thymus.

This study was performed to examine the presence and immunological properties of acetylcholine receptor (AChR) in rabbit thymus. Binding of 125I-alpha Bungarotoxin (alpha BGT) to Triton extract from rabbit thymus was saturable (half saturation value: 10 X 10(-9) M) and occurred with at least two affinities, a high one with a dissociation constant of 1.1 X 10(-10)M and a low affinity one with a dissociation constant of 2 X 10(-9)M. The complex formation of 125I-alpha BGT-thymus extract was inhibited by both carbamylcholine and D-tubocurarine. These results indicate the existence of AChR in rabbit thymus. Antibody to AChR which was purified from experimental myasthenic rabbits with Narke AChR-affinity gel and labelled with 125I was used to identify the receptor antigenicity in rabbit thymus. Specific binding of 125I-antibody to thymic extract was demonstrated by the DEAE-paper disc assay. It is concluded from these results that AChRs with a similar antigenicity to that of skeletal muscle AChR exist in rabbit thymus. Our findings obtained in this study will support a hypothesis that the primary immunogen in myasthenia gravis may be AChR in thymus and an autoimmune reaction against AChR might be initiated within the thymus gland itself.

Acetylcholine↗
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↗