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Biomedical subjects

A Noda

Publications and source records attributed to A Noda.

At least 181 records · Page 10Linked to original sources
PubMed1985

Elastase secretion in pancreatic disease.

To estimate the diagnostic value of elastase output in the duodenal aspirates during a pancreozymin secretin test, elastase as well as amylase, chymotrypsin, trypsin, and lipase was determined in 46 controls and 61 patients with various disease. The elastase output decreased significantly in chronic pancreatitis (mild exocrine insufficiency 13 and advanced eight), pancreatic cancer (n = 10), and liver cirrhosis (n = 14) when compared with the controls. The outputs of the four other enzymes also decreased in chronic pancreatitis and pancreatic cancer, not in liver cirrhosis. Low elastase output was found in four of 13 chronic pancreatitis patients with mild exocrine insufficiency, whereas low outputs of the other enzymes were observed in only one or less of the 13. The ratio of elastase to amylase alone was significantly lower in the pancreatic diseases. The results suggest that elastase is the most susceptible enzyme to pancreatic dysfunction and that its output and its ratio to amylase output provide a valuable index to assess the enzyme secretory capacity in the pancreatic diseases.

Cholecystokinin↗
PubMed1985

Differential determination of serum isoamylase using an amylase inhibitor and its clinical application.

Diagnostic significance of a simple and rapid screening procedure for determining the relative amounts of pancreatic and salivary isoamylase using an amylase inhibitor was evaluated in 242 subjects (controls 84, acute pancreatitis nine, chronic pancreatitis 28, pancreatic cancer 14, peptic ulcer 25, liver cirrhosis 15, cholelithiasis 24, irritable colon syndrome 13, diabetes mellitus 13, mumps seven, and chronic renal failure 10). Electrophoretically separated isoamylases of saliva and pure pancreatic juice were all inhibited at similar degrees to the corresponding unfractionated amylases. Total amylase and pancreatic isoamylase were elevated in all nine patients with acute pancreatitis. Pancreatic isoamylase was decreased in 12 of 28 patients (43%) with chronic pancreatitis and increased in nine of 14 patients (64%) with pancreatic cancer. The mean pancreatic isoamylase activity in the patients with acute pancreatitis was significantly higher (p less than 0.01), while that of chronic pancreatitis was significantly lower (p less than 0.05) when compared with controls. The inhibition method offers simple, rapid, and specific analysis of serum isoamylase for the differential diagnosis of hyperamylasemia in cases of emergency.

Adolescent↗
PubMed1984

Hyperamylasemia with papillary serous cystadenocarcinoma of the ovary.

A case of a 49-year-old housewife with persistent hyperamylasemia, intractable amylase-rich ascites, and papillary serous cystadenocarcinoma of the ovaries is presented. The hyperamylasemia was attributable to neoplastic production of salivary-type isoamylase by analysis of isoamylase in the serum, urine, ascites, primary tumor of the ovaries and metastatic tumor of the lymph nodes. Cellular localization of amylase in the tumor tissues was demonstrated immunohistochemically in the primary and metastatic tumors using an indirect immunoperoxidase method.

Amylases↗
PubMed1984

Metabolic hydrolysis of isoniazid by subcellular fractions of rat liver.

The characteristics of isoniazid amidase which hydrolyzes isoniazid to isonicotinic acid and hydrazine was examined in vitro using rat liver subcellular fractions. The activity of isoniazid amidase was estimated from the amount of hydrazine produced from a substrate, isoniazid, by means of GC-MS. High activity of the amidase was observed in the microsomal and lysosomal fractions, and at pH 7.4-7.8 in the microsomal fraction. The amidase was not inhibited by acetanilide, but by procaine and bis(p-nitrophenyl)phosphate. As expected, acetylisoniazid, a main metabolite of isoniazid, also inhibited the amidase. Not only the microsomal monooxygenase but also amidase was strongly induced by pretreatment with phenobarbital, 3-methylcholanthrene and rifampicin, respectively.

Amidohydrolases↗
PubMed1984

The excretion of dimethadione in pure pancreatic juice and bile in postoperative patients.

The excretion of dimethadione (DMO) in pure pancreatic juice and bile was studied in postoperative patients undergoing external drainage of pancreatic juice and in those who had undergone percutaneous transhepatic cholangiodrainage. During and after oral administration of trimethadione, which is the precursor of DMO, pancreatic DMO concentration closely paralleled plasma DMO concentration. Pancreatic juice/plasma concentration ratio for DMO exceeded 1.0. In a patient with a large pancreatic cyst communicating with the main pancreatic duct, pancreatic DMO concentration after single rapid injection of secretin inversely correlated with the flow rate, while its output depended directly on the rate. Biliary DMO output after secretin injection was closely dependent on the flow rate, but was extremely low. The present results are essentially compatible with the findings previously observed in dogs.

Adult↗
PubMed1984

Improved purification and enzymatic properties of three forms of reverse transcriptase from avian myeloblastosis virus.

The purification procedure for quantitative recovery of the three molecular forms, alpha, alpha beta and beta 2 of avian reverse transcriptase (Ueno, A., Ishihama, A. and Toyoshima, K. (1982) J. Biochem. 91, 311-322) was improved with respect to removal of nucleases. The three enzyme forms were prepared from avian myeloblastosis virus by CsCl centrifugation and poly(G)-agarose column chromatography. The alpha- and alpha beta-forms of the enzyme were further purified to near homogeneity by column chromatography on heparin agarose and DNA cellulose, respectively. The three enzyme forms thus purified were equally active in influenza virus RNA-directed synthesis of single-strand cDNA. By contrast, the alpha-form enzyme was more active in the single-strand cDNA-directed synthesis of double-strand DNA than the other two enzyme forms.

Avian Leukosis Virus↗
PubMed1983

Is isoniazid-hepatotoxicity induced by the metabolite, hydrazine?

The effects of rifampicin (RMP) on isoniazid (INH) metabolism in rabbits were examined from the viewpoint of extensive hepatitis. After the RMP pretreatment, no remarkable changes were observed in the plasma levels of INH as well as its metabolites, acetylisoniazid (AcINH), acetylhydrazine (AcHz) and diacetylhydrazine (DAcHz) with the exception of hydrazine (Hz). After an oral administration of INH or Hz hydrate, the stochastic examination showed that the AUC0-8hr values of Hz plasma levels in RMP pretreated groups were significantly less than those in the control rabbits. RMP treatment was also shown to induce rabbit liver cytochrome P-450 activity. Histological studies demonstrated that Hz causes more remarkable hepatic necrosis in rabbits pretreated with RMP than in the control rabbits. These observations could suggest that Hz is a key intermediate of INH-hepatitis through the transformation of some hepatotoxic species by microsomal oxidation that is facilitated by RMP.

Animals↗