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Biomedical subjects

N Kikuchi

Publications and source records attributed to N Kikuchi.

At least 181 records · Page 10Linked to original sources
PubMed1987

Exercise-induced changes in branched chain amino acid/aromatic amino acid ratio in the rat brain and plasma.

Central fatigue was induced by running rats on a treadmill. Amino acid and ammonia metabolism in the brain and blood were followed with time to correlate its changes with physical exhaustion. The blood ammonia level did not change during running, but was prominently increased at exhaustion. The brain level of ammonia was also prominently high at the end of exercise with a time course of change similar to that of the blood level. Plasma concentrations of branched chain amino acids (BCAA) and aromatic amino acids (AAA) increased as the animals continued to run; however, the plasma BCAA/AAA ratio was definitely depressed at exhaustion. This was also true with the brain BCAA/AAA ratio. A positive correlation was demonstrated between the plasma and brain BCAA/AAA ratios at r=0.5040 and P less than 0.05. These exercise-related changes suggest that physical exercise-induced central fatigue involves not only an increase in brain ammonia, but also a disturbance in brain amine metabolism accompanying plasma and brain BCAA/AAA ratio depression. Furthermore, the ammonia level and BCAA/AAA ratio in the brain correlated with those in the blood. It is reasonable to consider that the blood ammonia concentration and plasma BCAA/AAA ratio may serve as important indices of the clinical condition of exercise-induced central fatigue.

Amino Acids↗
PubMed1987

[Clinical studies of norfloxacin on respiratory tract infections in aged people].

Norfloxacin (NFLX), an oral antibacterial agent of new quinolone derivative, was administered at daily doses of 300-600 mg t.i.d. to 20 aged patients with respiratory tract infections. The results obtained are summarized as follows. 1. Clinical efficacies were moderate in 6 patients with upper respiratory tract infections, and moderate in 11 patients and fair in 3 patients with lower respiratory tract infections. In the 20 patients, overall clinical efficacies were moderate in 17 patients, hence the efficacy rate was 85%. 2. Bacteriologically, causative organisms were detected in 10 of the 14 cases with lower respiratory tract infections. In these cases, bacteriological responses were "eradicated" in 9 cases, "decreased" in 1 case and "unknown" in 1 case, the rate of eradication was 90%. 3. No adverse reactions or abnormal laboratory test values were observed.

Aged↗
PubMed1986

Purification and characterization of recombinant murine immune interferon.

The recombinant murine immune interferon (rMu-IFN-gamma) was purified to homogeneity from Escherichia coli harboring the expression vector of murine IFN-gamma. The purified rMu-IFN-gamma showed an Mr of 15 000 in SDS-polyacrylamide gel electrophoresis. Results of amino acid analysis, amino- and carboxyl-terminal analyses and peptide mapping of rMu-IFN-gamma suggest that it has the complete protein sequence predicted on the basis of cDNA except for lack of four amino acid residues from the mature carboxyl-terminus.

Amino Acid Sequence↗
PubMed1986

Monoclonal antibodies distinguish between the head portions of two myosin isozymes from chicken breast muscle.

Monoclonal antibodies against chicken breast myosin and its subfragment-1(S-1) were produced. One antibody, 2G41, reacted with S-1 containing a light chain 3 (LC3), but not with another S-1 containing a light chain 1 (LC1) or a mixture of the light chains. A structural difference can be assumed to exist between the head portions of the two myosin isozymes. Antigenicity of S-1 toward 2G41 could not be detected after tryptic digestion into three fragments of 50K, 27K, and 20K daltons. Another monoclonal antibody, M68, was obtained from mice immunized with myosin. M68 preferably recognized the heavy chain from S-1 containing LC3 rather than that from that containing LC1 or S-1. M68 reacted with the 27K fragment among the three.

Animals↗
PubMed1986

[Doppler evaluation of porcine mitral valve dysfunction].

Seventy patients with bioprosthetic mitral valve were examined to study the applicability of the Doppler techniques including pulsed, continuous wave and color Doppler echocardiography in diagnosing and evaluating the severity of prosthetic valve dysfunction. The study population consisted of 70 patients who underwent mitral valve replacement (45 patients with Hancock valve, 13 with Angell-Shiley valve, 10 with Carpentier-Edwards valve). The dysfunctions were transvalvular regurgitation in 20 instances and paravalvular regurgitation in three, all of which were confirmed at surgery. A control group of 47 patients with the normally functioning porcine prosthetic mitral valve were also studied. Diastolic transmitral flow patterns were recorded from parasternal and apical approaches using color Doppler echocardiography, and the direction of the flow was definitely identified on the flow image. Transmitral flow signals spread from the mitral orifice to the mid-portion of the interventricular septum, and its direction was perpendicular toward the mitral ring in all cases. Flow velocity patterns in the left ventricle and atrium were recorded in the apical long-axis view of the left ventricle or apical four-chamber view using pulsed (high pulse repetition frequency) and continuous wave Doppler techniques. Two dynamic alterations in patients with the porcine mitral valve were evaluated from 1) the peak velocity and pressure half time (PHT) of transmitral flow in early diastole, and 2) the regurgitant jet in the left atrium indicating transvalvular or paravalvular regurgitation. The results were as follows: 1. Normally functioning porcine mitral valves were characterized by peak velocities (PV) less than or equal to 1.82 (mean +/- SD 1.44 +/- 0.27) m/sec and PHT less than or equal to 180 (mean +/- SD: 135 +/- 30) msec. In 23 patients with prosthetic valve dysfunction documented at surgery, peak velocity (mean +/- SD 2.23 +/- 0.19 m/sec) was significantly greater (p less than .001) than that of patients in the normally functioning prosthetic valves, and PHT ranged from 135 to 340 msec (mean +/- SD: 226 +/- 81 msec). 2. Among the 23 patients with porcine valve dysfunction, a harmonic striped pattern were recorded at the mitral valve levels in eight patients. All these patients had a musical murmur, and their peak velocity was more than 2.0 m/sec, but the PHT was less than 180 msec in seven patients. In these patients, valvular tears without calcification were confirmed at surgery.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1985

Purification and complete amino acid sequence of canine pancreatic secretory trypsin inhibitor.

Pancreatic secretory trypsin inhibitor (PSTI) was purified from canine pancreatic juice by HPLC. Canine PSTI inhibited bovine trypsin activity stoichiometrically and strongly with a dissociation constant of below 10(-9) M. The amino acid sequence of canine PSTI was determined by conventional methods. It had one more amino acid residue at the amino-terminus than other mammalian PSTIs, i.e. human, porcine, bovine and ovine.

Amino Acid Sequence↗
PubMed1985

The multiplicity of human pancreatic secretory trypsin inhibitor.

Four forms of pancreatic secretory trypsin inhibitor (PSTI; A1, A2, B, and C) were purified from human pancreatic juice. According to sequence results, the primary structure of B was different from that reported earlier (Greene, L.J., et al. (1976) Method Enzymol. 45, 813-825) at two positions, i.e. Asn21----Asp21, Asp29----Asn29. A1 and A2 were deamidated forms of B judging from peptide mappings with Staphylococcus aureus V8 protease. Gln45 in B was replaced by Glu in A1 and Gln51 in B was replaced by Glu in A2. C was an inhibitor lacking five amino acid residues from the amino terminal of B. B and C inhibited human cationic trypsin activity stoichiometrically with similar dissociation constants, but A1 and A2 showed poorer trypsin inhibitory activity than B and C.

Amino Acid Sequence↗
PubMed1985

Structures of sugar chains of the third component of human complement.

Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components. The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated. The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography. The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis. These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2. Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.

Acetates↗