[Radiologic diagnosis of malignant lymphoma of the large bowel (author's transl)].
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Biomedical subjects
Publications and source records attributed to K Ninomiya.
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Occlusive intracoronary (IC) thrombosis was produced experimentally in dogs by placement of a copper coil. The thrombus was consistently lysed by application of Thrombolysin (streptokinase and plasminogen) at the site of occlusion, 1 to 6 hours after thrombosis. Thrombolysin has no toxic effect on the coronary artery wall or the myocardium. Reperfusion after 30 to 60 minutes of occlusion frequently resulted in ventricular fibrillation, but gradual reperfusion reduced the probability of ventricular fibrillation. Intramyocardial bleeding was noted after reperfusion in areas of advanced necrosis and was shown to be the consequence, rather than the cause, of necrosis. The reperfused myocardium remained hypocontractile, but in contrast to the occlusion period, its mechanical function could be enhanced by inotropic stimulation. After experimental studies confirmed the feasibility and safety of IC thrombolysis, the technique was applied within 3 hours of onset of pain in 29 patients with evolving acute myocardial infarction (AMI) and showing ST elevations without pathologic Q waves. Nitroglycerin (NTG), 0.1 mg, was injected into the occluded coronary artery to rule out spasm; NTG failed to open the occluded artery. A special, very flexible, radiopaque No. 2 French catheter was advanced through the angiography catheter to the site of occlusion. Thrombolysin was infused at a rate of 4000 to 6000 IU/min until patency was achieved, followed by 2000 IU/min for 60 minutes. Lysis of clot was achieved in 27 of 29 patients. The single death (unrelated to the procedure) occurred subsequently in a patient in whom the artery was not reopened. After successful thrombolysis, 12 patients underwent elective coronary bypass surgery because of multiple stenoses. The need for early reperfusion is emphasized for effective IC thrombolysis therapy in evolving AMI.
The right ventricular ejection fractions derived from two dimensional echocardiograms and cineangiograms were compared in 24 children. All patients (aged 2.1 to 16 years) had undergone Mustard repair for transposition of the great arteries 1 to 12 years earlier. The correlation of the two methods was excellent (r = 0.977), confirming the usefulness of echocardiography for deriving ejection fraction. The volume components of the ejection fraction were less well estimated from the echocardiograms, but the ratios of end-diastolic to end-systolic volumes estimated from each method were similar.
An aminopeptidase was purified about 1,700-fold from seeds of Japanese apricot (Prunus mume Sieb.) by a seven-step procedure comprising extraction from seeds, ammonium sulfate fractionation, DEAE-cellulose chromatography, first and second DEAE-Sepharose chromatography, hydroxyapatite chromatography, and Sephadex G-200 gel filtration. The purified enzyme was shown to be homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 56,000 by gel filtration on Sephadex G-200 and the isoelectric point was 4.9. The pH optimum for L-leucine beta-naphthylamide was between pH 6.5 and 7.0, and the enzyme was stable in the pH 5.0 to 8.3 region and up to 50 degrees C. The enzyme hydrolyzed a variety of aminopeptidase substrates with a free alpha-amino group. Of the amino acid beta-naphthylamides, the enzyme was highly specific for substrates with a hydrophobic side chain in the amino terminal residue. The enzyme was strongly inhibited by p-chloromercuribenzoate, heavy metals, diethyl pyrocarbonate, and photooxidation with methylene blue, but was not affected by thiol compounds, peptidase inhibitors of microbial origin, such as bestatin and puromycin, or metal chelating agents. No activation of the enzyme by metal ions was observed. These results suggest that the enzyme is a true aminopeptidase in which cysteine and histidine residues participate in the catalytic process, and is not classifiable as a metalloenzyme.
Fundamental and clinical studies of cefotaxime (CTX), a new semisynthetic cephalosporin antibiotic were carried out in the field of obstetrics and gynecology. The following results were obtained. 1. CTX was almost equally active to SCE-1365 and less active than cefotiam (CTM) and cefazolin (CEZ) against S. aureus, much more active than these 3 antibiotics against E. coli, more active than the 3 antibiotics against Enterobacter, equally active to SCE-1365 and a little weaker than CEZ against anaerobic Gram positive cocci, and superior to SCE-1365 and CEZ against Bacteroides. 2. CTX was more stable to B. fragilis-producing beta-lactamase than CET, CEZ and cefoperazone (CPZ). 3. The concentrations of CTX transferred to the female genital organs after CTX 1 g d. i. were sufficiently effective against facultative or strict anaerobic bacteria mainly isolated from obstetrical and gynecological infections. 4. CTX was administered to 10 patients with genital infections. CTX was excellent in 1 case, good in 8 cases and poor in 1 case. The response rate of CTX was 90%. Bacteria, isolated in 5 cases before CTX treatment, were eradicated in 4 cases. The bacteriological effectiveness of CTX was thus 80%. 5. No side effect attributable to CTX was observed.
A fundamental and clinical study of ceftizoxime (CZX), a new cephalosporin antibiotic, has brought about the following results. 1. The antibacterial activity of CZX against Bacteriodes fragilis and B. thetaiotaomicron was superior to that of CEZ, but inferior to that of CFX. CZX was the most active of the 3 drugs against B. distasonis, and was as active as CFX against B. vulgatus. The MICs of CZX against Peptococcus, Peptostreptococcus and anaerobic Streptococcus were 1.56 microgram/ml or lower. CEZ was more active than CZX against these anaerobic cocci. 2. The concentrations of CZX in female genital organs and retroperitoneal dead space exudate after drip infusion of 1 g were high enough to fulfill the MICs of many bacterial isolates. 3. CZX administered intravenously to 9 patients in daily doses of 1 approximately 8 g for 4 approximately 11 days was 100% effective. Pathogenic bacteria in 6 of the patients were eradicated in 4 and partially eradicated in 1. The other patient had no bacteriological examination after therapy. 4. No adverse reaction was observed. From above results it is concluded that CZX must be one of the most effective antibiotics for the treatment of gynecological infections.
An aminopeptidase B from porcine liver was purified about 2,000-fold by ammonium sulfate fractionation and a series of chromatographies on hydroxyapatite, DEAE-cellulose, Sephadex G-150, hydroxyapatite and DEAE-Sepharose columns. The purified preparation was homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was about 58,000 as determined by gel filtration on Sephadex G-100 and disc gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme exhibited maximum activity at pH 7.5 for the hydrolysis of L-arginine beta-naphthylamide at 25 degrees C. The enzyme was labile to prolonged warming and freezing. The enzyme was markedly stimulated by chloride ion, and was inhibited by Cu2+, Zn2+, Cd2+, Hg2+, Pb2+, and metal chelating agents. p-Chloromercuribenzoate was an uncompetitive inhibitor of the enzyme with a Ki value of 1.8 X 10(-6) M. The enzyme was inhibited by 1,10-phenanthroline and the inhibition was of the mixed type with a K1 value of 1.9 X 10(-4) M but activity was restored by the addition of Zn2+, Co2+, and Fe2+.
Porcine liver aminopeptidase B[EC 3.4.11.6] is highly specific for hydrolysis of beta-naphthylamides of basic L-amino acids; the Km values for L-arginine beta-naphthylamide and L-lysine beta-naphthylamide were 0.035 and 0.12 mM, respectively. The enzyme was inhibited by various alpha-amino acids. Among basic amino acids, L-homoarginine and L-arginine were the most potent inhibitors, L-lysine and L-norarginine (alpha-amino-gamma-guanidinobutyric acid) being less inhibitory. Hydrophobic amino acids also inhibited the enzyme competitively. This suggests that there is a hydrophobic region that binds the side chain of the substrates or inhibitors in the specificity site of the enzyme. Studies on the inhibitions by L-arginine derivatives showed that blocking of the alpha-carboxyl or the alpha-amino group reduced the inhibitory effect of L-arginine. Porcine liver aminopeptidase B was not inhibited by puromycin, whereas bestatin inhibited the enzyme competitively with a Ki value of 1.4 X 10(-8) M. This enzyme had no kinin-converting activity.
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The following results were obtained from the comparison of cefoperazone (CPZ) with cefazolin (CEZ), cephalothin (CET) and cefoxitin (CFX) in respect to their antibacterial action against anaerobic bacteria: 1) CPZ showed an antibacterial spectrum which was comparable to those of the known antibiotics, CEZ, CET and CFX. CPZ was particularly effective against anaerobic Gram-positive bacteria. 2) CPZ showed a distribution of susceptibility against clinically isolated strains which was comparable to those of CEZ, CET and CFX, CPZ was slightly inferior to CFX against B. fragilis and B. thetaiotaomicron, but was somewhat superior to any of CEZ, CET and CFX against anaerobic Gram-positive rods and B. distasonis. 3) The susceptibility of B. fragilis and F. necrophorum to CPZ decreased with an increase in the amount of inoculation, while C. perfringens and P. asaccharolyticus did not show any difference in susceptibility with the amount of inoculation. 4) The values of MIC and MBC of CPZ showed good coincidence with each other, thereby testifying its superior bactericidal action. 5) Natural resistant mutants were not obtained. 6) According to the examination of resistance in a test tube, P. variabilis did not show any appreciable increase in resistance, but F. varium increased its resistance rapidly. 7) CPZ was inferior only to CFX in stability against the beta-lactamase of B. fragilis. All of CEZ, CET and CMD lacked stability against the beta-lactamase of B. fragilis. 8) CPZ was found effective for the treatment of experimental subcutaneous abscess in mice caused by F. necrophorum.
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