牛乳中のプラスミノゲン・アクチベーターの分離と分娩後の動態

Plasminogen activator was separated by gel-filtration of skimmed milk from bovine until 9^ day after delivery. The separation pattern of plasminogen activator in bovine milk was different from one of human milk. The activities of plasminogen activator in bovine milk were compared among three groups of skimmed milk samples obtained in 1～3day, 4～6day, 7～9day after delivery. The mean value for each group were 3.2IU/ml(l～3day), 3.5IU/ml(4～6day) and 0.3IU/ml(4～9day)

基質を含むポリアクリルアミド・ゲル電気泳動法によるヒト血漿中の中性セリンプロテイナーゼの検出の試み

In order to examine the existence of proteinase in the human plasma, the electrophoretic method by using polyacrylamide-gel containing SDS and substrate was adopted in this study. The proteinase-like substance in the human plasma hydrolyzed fibrinogen, gelatin and α-casein, but did not the serum albumin, the hemoglobin and γ-globulin. The fibrinogenolytic activity in the human plasma was detected in all of six healthy subjects. The activity was disappeared at 50℃ for 30min, and inhibited by 10^M DFP or anti-human plasminogen IgG. The proteinase-like substance was bound on lysine-Sepharose CL-4B and eluted with 0.2M ε-aminocaprylic acid. The examination by gel filtration induced that the fibrinolytic activity existed in the fraction corresponding to the molecular weight of 90kDa. By the immunoblotting method, a mobility of the substance was shown to be similar to that of human plasminogen. The data demonstrated that the plasmin-like proteinase activity in the human plasma was artifact something made from plasminogen

全血と血漿の凝固時間に対する採血後の保存時間の影響

Obtaining a sufficient volume of blood for research purposes from small animals, such as mice, is difficult, especially because usually only the plasma is used for various tests. The ideal solution would be to use the whole blood for measurements such as that of coagulation time. Being able to use the whole blood sample would double the amount available for tests and also should provide an environment closer to that in the living organism. However, the questions arise of whether differences exist between the coagulation time of whole blood and plasma and what the effects of storage time are. We examined these issues and found that both the whole blood and plasma could be used for measurement of thrombin time, activated partial thromboplastin time and prothrombin time

An Improved Convenient Molecular Weight-determination Method of Subunit for Active Stainable-Enzyme after SDS Electrophoresis

An improved method to determine the molecular weight of the subunit of lactate dehydrogenase and malate dehydrogenase after sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) has been developed. This method was based on the finding that on a gel, which was washed with a buffer to remove SDS after SDS-PAGE, stained with an enzymatic activity staining mixture and then stained with coomassie blue, there appeared one active stained band with apparent molecular weights of 35,500 (monomer) (lactate dehydrogenase) and 31,000 (monomer) (malate dehydrogenase) on the SDS-PAGE gel. The method developed here may be applicable to a wide range of active stainable-enzymes as a rapid and simple molecular weight determination method of the subunit after SDS-PAGE

An Improved Convenient Molecular Weight-determination Method for Active Stainable-Enzyme after SDS Electrophoresis

An improved method to determine the molecular weight of alcohol dehydrogenase after sodium dodecylsulfate polyacrylamide gel electrophoresis(SDS-PAGE) has been developed. This method was based on the finding that on a gel, which was washed with a buffer to remove SDS after SDS-PAGE, stained with an enzymatic activity staining mixture and then stained with coomassie blue, there appeared two active stained bands with apparent molecular weights of 148,000(tetramer)and 35,000(monomer)on the SDS-PAGE gel. The method developed here may be applicable to a wide range of active stainable-enzymes as a rapid and simple molecular weight determination method after SDS-PAGE

絶食後の種々の糖質摂取が筋肉および肝臓のグリコーゲン量に及ぼす影響

The mice were dosed with several sugars (glucose, maltose, starch, sucrose, lactose) by ingestion after fast for 24 hours, and the changes of blood sugar level, glycogen concentration in the liver and muscle were examined according to time-schedule. The level of glycogen in muscle by the fast for 24 hours was consumed more than the ones of blood-sugar and liver-glycogen. The level of blood sugar was recovered immediately after dose of sugars by ingestion, and the synthesis of liver-glycogen and muscle-glycogen were followed. The synthesis of muscle-glycogen after recovery of blood sugar by glycogen-dose was more remarkable than others

エンドトキシン誘発播種性血管内凝固に対する糖尿病の影響

This paper is a study concerning diabetes that have a tendency for blood coagulation whether it was a risk of sudden death. We made a diabetes model mouse by intraperitoneal injection of streptozotocin (STZ), and we caused disseminated intravascular coagulation (DIC) by doing an intra-tailvenous injection of endotoxin (ET) to the mouse. After injection of STZ, a weight loss, decrease of intra-abdominal fat, polyphagy, polyposia are induced and they are the main symptoms of diabetes. Furthermore, with an ET injection to the mouse, it showed increase of weight such as the lung and the liver and extension of PT time with the blood clot formation, and that it was it in a blood coagulation tendency was confirmed by these symptoms. Then, the mouse showed a decrease of plasminogen activator activity in the lung. Therefore, fibrinolysis system was enhanced in the mouse, and it was suggested that a symptom of DIC turned worse under a state of diabetes

カラゲニン誘発炎症におけるフィブリノゲンならびにプラスミノゲン分解酵素活性についての研究

This paper is a study concerning plasminogenolytic and fibrinogenolytic products in plasma. Two types of the spleen or the lung were made preparation for this study. One type is the spleen or the lung on 10th day after carrageenan injection, and non treated ones. The plasminogenolytic and fibrinogenolytic activities in plasma were increased by carrageenan induced inflammation. These digested products with the spleen or the lung are similar to ones with commercial cathepsin G. We came to conclusion that the plasminogen degradated products in plasma were ones by cathepsin G in the lung or the spleen