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Biomedical subjects

H Urabe

Publications and source records attributed to H Urabe.

At least 91 records · Page 5Linked to original sources
PubMed1978

Essential IgG cryoglobulinemia with purpura and cold urticaria.

An 80-year-old woman with essential cryoglobulinemia developed recurrent, widespread, purpuric lesions with superficial skin ulcers and cold urticaria. No disorders of other organ systems were recognized. Attempts to transfer the cold sensitivity passively by serum and isolated cryoprecipitate of the patient were successful. Immunochemical studies showed that the cryoglobulin was composed of IgG only. It was suggested that the cryoprecipitate might not be due to immune complex formation in this case.

Adrenal Cortex Hormones↗
PubMed1977

Immobilization of urea cycle enzymes. I. Characterization of immobilized carbamoylphosphate synthetase and ornithine carbamoyltransferase.

Carbamoylphosphate synthetase (EC 2.7.2.5) and ornithine carbamoyl-transferase (EC 2.1.3.3) extracted from frog liver were successfully immobilized on CNBr-activated Sepharose 4B. The immobilized preparation had a better stability towards heat. The apparent Michaelis constant values for N-acetylglutamate, ammonia, and ATP were not significantly changed by immobilization.

Animals↗
PubMed1977

Immobilization of urea cycle enzymes. II. Characterization of immobilized argininosuccinate synthetase.

Argininosuccinate synthetase (EC 6.3.4.5) was immobilized on CNBr-activated Sepharose 4B. Properties of the immobilized enzyme are described and compared with those of the native enzyme. The immobilized enzyme was much more stable than the native enzyme at 37 degrees C. It was further stabilized in the presence of the assay reagents. The optimum pH of the immobilized enzyme shifted towards alkalinity (approximately 0.5 unit). The apparent Michaelis constants measured for the immobilized enzyme were not greatly different from those measured for the native enzyme. Urea formation from citrulline was confirmed in a continuous column reactor by the coimmobilized argininosuccinate synthetase, argininosuccinate lyase (EC 4.3.2.1), and arginase (EC 3.5.3.1).

Animals↗
PubMed1977

Purification and characterization of guinea-pig epidermal acid phosphatase.

Guinea-pig epidermal acid phosphatase has been purified approximately 120-fold by a procedure including acid treatment, CM-cellulose and DEAE-cellulose chromatography, and gel filtration on Sephadex G-100. The enzyme had a pH optimum at 5-0 and the optimal temperature for activity was approximately 50 degrees C. The enzyme was not activated by divalent cations or 2-mercaptoethanol, but it was inhibited by p-chloromercuribenzoate and by fluoride. The km value for p-nitrophenyl phosphate was 1-31x10-4 M, the molecular weight was about 73,000 as determined by Sephadex G-100 gel filtration and the isoelectric point was 6.1. The enzyme hydrolyzed deoxyribonucleoside monophosphates to deoxyribonucleosides.

Acid Phosphatase↗
PubMed1976

Perioral dermatitis and rosacea-like dermatitis: clinical features and treatment.

Nine cases of perioral dermatitis and 16 cases of rosacea-like dermatitis have been treated for the last 3 years at our clinic. These cases were all females whose ages ranged from 18 to 61 years with a mean of 45 years. All had been under treatment with fluorinated steroids for a period of from 3 months to 10 years, about 3 years on the average. Tetracyclines were beneficial as remedies for these conditions, bringing about healing or remission in approximately 3 months. About 1 year was required for the recovery from atrophy of the skin and telangiectasia. Hydrocortisone 17-butyrate was more useful as a topical medication than hydrocortisone acetate but gave rise to withdrawal rebound eruptions in some cases.

Administration, Oral↗
PubMed1975

Degradation of deoxyribonucleic acid by guinea pig epidermal extracts.

The capability of guinea pig epidermal extracts to hydrolyze deoxyribonucleic acid has been studied. The results of investigation by gel filtration on Sephadex G-75 column and by viscometry on the mode of hydrolysis of deoxyribonucleic acid by epidermal extracts revealed that deoxyribonucleic acid was degraded by both endonuclease and exonuclease activities. The exhaustive digestion by epidermal extracts yielded the complete degradation of deoxyribonucleic acid to mononucleosides or further metabolites. The enzyme systems involved in the deoxyribonucleic acid degradation include at least an endonuclease, an exonuclease and a phosphatase.

Animals↗