A 51-year-old man had excruciating pains in the left arm and chest approximately four weeks after ingestion of live loaches. Eosinophilia, eosinophilic pleocytosis in the CSF, and a high serum IgE level were noted. Skin tests and antigen-antibody reactions were positive for Gnathostoma infection. His clinical signs and symptoms ameliorated with symptomatic treatment within six months. Only 34 cases of gnathostomiasis involving the CNS have been reported in the English literature, and ours is the first Japanese case, to the best of our knowledge, of eosinophilic meningoradiculomyelitis caused by Gnathostoma spinigerum.

Eosinophilia↗

PubMed1983

[2 cases of aortic dissection during cardiopulmonary bypass via femoral arterial cannulation and its etiology].

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Aortic Dissection↗

PubMed1982

[Successful surgery of an anomalous origin of the left coronary artery at the pulmonary artery--reconstruction of the left coronary artery using a free segment of the subclavian artery].

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Child↗

PubMed1978

Possible participation of glucocorticoid in elevation of 3',5'-cyclic AMP levels through inhibition of cyclic AMP phosphodiesterase.

Administration of prednisolone and cholate to rats elevated levels of cAMP (adenosine 3',5'-cyclic monophosphate) by 1.5- to 2.0-fold. Compounds such as prednisolone, hydrocortisone, cholate, and deoxycholate were found to be potent inhibitors of partially purified cAMP phosphodiesterase prepared from rat liver. Kinetic analysis showed that the prednisolone inhibition was noncompetitive with a Ki of 8.9 x 10(-4) M. These results suggest that in addition to increasing DNA-dependent RNA polymerase activity in vivo, a large application of glucocorticoid may incur elevation of intracellular cAMP levels.

3',5'-Cyclic-AMP Phosphodiesterases↗

PubMedDate not supplied

Sensitive enzyme immunoassay of cephalexin residues in milk, hen tissues, and eggs.

A sensitive enzyme immunoassay for cephalexin (CEX) was developed using the rabbit antiserum to CEX, beta-D-galactosidase-labeled CEX, and a double-antibody separation method. The immunogen of CEX was prepared by coupling the amino group of CEX to thiol groups introduced into bovine serum albumin by the use of N-(m-maleimidobenzoyloxy)succinimide as a cross-linker. Highly titered antiserum to CEX was produced in rabbits immunized with the immunogen. Enzyme labeling of CEX with beta-D-galactosidase was done by using N-(gamma-maleimidobutyryloxy)succinimide as the cross-linker. The limit of detection was 30 ng CEX/mL sample solution. Application of the method to CEX drug residues detected 30 ng/mL in milk, 60 ng/g in egg yolk, and 400 ng/g in hen tissue.

Animals↗