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Biomedical subjects

A Funakoshi

Publications and source records attributed to A Funakoshi.

At least 253 records · Page 14Linked to original sources
PubMed1980

Biochemical and clinical studies on human pancreatic deoxyribonuclease I inhibitor.

Human pancreatic Deoxyribonuclease I (DNase I), inhibitor was partially purified from duodenal juice of healthy subjects collected in the Pancreozymin-Secretin test, by a procedure which included ammonium sulfate fractionation, DEAE cellulose fractionation, Sepharose 4B affinity chromatography, and gel filtration. The final preparation inhibited DNase I only, and had no inhibitory activity on pancreatic RNase, and trypsin. The inhibitor had a molecular weight of approximately 40,000, as determined by gel filtration, and showed the same mobility as skeletal muscle actin on SDS gel electrophoresis. Then clinical studies were made on the DNase I inhibitor in duodenal juice obtained after administration of Pancreozymin and Secretin to patients with various pancreatic diseases. In patients with suspected chronic pancreatitis with whom the ordinary test, containing the assay of the total volume, amylase output and maximum bicarbonate concentration of duodenal juice had produced normal results, the DNase I inhibitor output was observed to be higher than that in control subjects. While it was lower in patients with confirmed chronic pancreatitis than in control subjects. There results imply that DNase I inhibitor output may be an indicator of the pancreatic inflammation state and be useful for the early detection of pancreatic diseases.

Cholecystokinin↗
PubMed1980

Simple purification and properties of bovine pancreatic deoxyribonuclease I.

A simple purification method for pancreatic deoxyribonuclease I (DNase I) [EC 3.1.4.3] was developed by utilizing the technique of isoelectric focusing. The active protein was resolved in to at least four forms with different isoelectric points; the major components a, b, and c had isoelectric points at pH 5.2, 4.9, and 4.8, respectively, and that of the minor component d was at 4.7. The four components (a, b, c, and d) exhibited peaks similar to those observed by Salnikow et al. after phosphocellulose chromatography (A, B, C, and D). The four components were all free from RNase and protease activities and were very stable at 0-2 degrees C for at least four weeks. Further, each of the four peaks exhibited a single protein band after polyacrylamide electrophoresis. DNase I-a antibody was prepared; it was very specific for DNase I and precipitated with the other components (b, c, and d). The mode of endonucleolytic action of pancreatic DNase I-a purified from Worthington DP grade DNase I was investigated. The sedimentation patterns in neutral sucrose gradients of digest of circular duplex DNA in an early stage of hydrolysis suggested that DNase I produces single strand scissions in the initial attack in the presence of divalent metal ions.

Animals↗
PubMed1979

Clinical studies on carcinoembryonic antigen in pancreatic cancer.

We studied serum carcinoembryonic antigen (CEA) levels in 82 patients. Thirty-four of these had benign diseases while 48 had malignant diseases. Highest incidence and levels of CEA occurred in the sera of patients with pancreatic cancer and stomach cancer. In this paper we focused our particular attention on the serum CEA of 25 pancreatic cancer patients, and examined differences in serum CEA levels in relation to histologic differentiation and sites of pancreatric cancer. No statistical difference in serum CEA level was found among various histologic types and sites of the pancreatic cancer. Clinical courses of two patients with pancreatic cancer were also studied. Serial determinations of CEA levels are most useful in assessing the effect of operation or chemotherapies and are a useful indicator for differentiating pancreatic cancer from chronic pancreatitis but cannot be a conclusive factor for the diagnosis. Finally, we correlated serum CEA levels with those of RNase and confirmed a positive correlation.

Carcinoembryonic Antigen↗
PubMed1979

Clinical investigation of serum deoxyribonuclease: I. Analysis of serum deoxyribonuclease activity in comparison with normal and after endoscopic retrograde pancreatography.

Serum Deoxyribonuclease (DNase) micro-assay method was developed using 32P-labelled E. coli DNA as substrate. The serum DNase showed maximum activity at pH 7.5. It required Mg+ for activity, and was inhibited by EDTA or EGTA. The enzyme was also inhibited by actin (60-65%) or bovine pancreatic DNase I antibody (40-45%). The serum DNase activity was markedly increased following endoscopic retrograde pancreatography (ERP) examination. These results imply that serum DNase activity is mostly at least 60-65% pancreatic DNase I.

Actins↗
PubMed1979

Clinical investigation of serum deoxyribonuclease: II. Clinical studies of serum deoxyribonuclease activity in pancreatic disease.

Serum Deoxyribonuclease (DNase) of normal persons and of patients with chronic pancreatitis, pancreatic cancer, Diabetes Mellitus, or other malignant diseases was determined with (32P) DNA as substrate. Serum DNase activity was much lower in patients with chronic pancreatitis, pancreatic cancer, or other malignant diseases than in control subjects, and serum DNase activity was almost normal in patients with Diabetes Mellitus. There was no correlation between serum DNase and serum amylase, but there was a good correlation between serum DNase and DNase I output in duodenal juice. There was an inverse correlation between serum DNase and serum RNase. These results imply that in the diagnosis of possible pancreatic disorders serum DNase may be a good indicator and thus may be useful for the detection of malignant diseases.

Amylases↗
PubMed1979

Clinical studies on human pancreatic deoxyribonuclease I.

Duodenal juice collected after administration of Boot's pancreozymin and secretin to patients with various pancreatic diseases was subjected to deoxyribonuclease I (DNase I) assay, as well as measurements of total volume, amylase output and maximum bicarbonate concentration. It was observed that the DNase I output is well correlated with each of three factors. The DNase I output was much lower in patients with chronic pancreatitis or pancreatic cancer than in control subjects, and DNase I output was even found to be low in patients suspected of having chronic pancreatitis, who did not give abnormal resulsts with other assay methods. These results imply that DNase I output may be a good indicator of exocrine function of the pancreas, and thus may be useful for early detection of pancreatic diseases.

Amylases↗
PubMed1978

Serum ribonucleases in pancreatic cancer: relation to tumor histology.

Serum Ribonuclease (RNase, EC. 3. 1. 4. 22) of normal persons and of patients with chronic pancreatitis, or pancreatic cancer was determined with poly (C) as substrate. Strikingly abnormal elevations occured in the serum RNase of patients with pancreatic cancer (p less than 0.001). Average serum RNase values of 18 normal persons, 10 patients with chronic pancreatitis and 26 patients with pancreatic cancer were 92, 118, and 249 units, respectively. In patients with pancreatic cancer, we compared the RNase level with four histologic types (ductar cell adenocarcinoma, anaplastic cell carcinoma, acinar cell carcinoma, and islet cell carcinoma). Adenocarcinoma showed higher activity than the other histologic types (p less than 0.005). When we compared the serum of pancreatic cancer and pancreatic cancer tumor extract with normal serum and normal pancreas extract, strikingly different phosphocellulose chromatographic pattern were evident. The correlation of increased serum RNase levels with tumor histology and different chromatographic pattern may explain the new enzyme production in cancer patients, and have biological significance in the development of pancreatic cancer.

Adenoma, Islet Cell↗