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Thromb Haemost 1981; 45(02): 121-126
DOI: 10.1055/s-0038-1650147
Original Article
Schattauer GmbH Stuttgart

Plasminogen-Activator in Human Early Milk: Its Partial Purification and Characterization

Utako Okamoto
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University, Kobe, Japan
,
Noboru Horie
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University, Kobe, Japan
,
Yoko Nagamatsu
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University, Kobe, Japan
,
Jun-Ichiro Yamamoto
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University, Kobe, Japan
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Further Information

Publication History

Received 07 July 1980

Accepted 16 January 1981

Publication Date:
05 July 2018 (online)

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Summary

Milk plasminogen-activator was partially purified from human transitional milk collected at about 10 days after delivery, by a five-step procedure involving chloroform treatment, ammonium sulfate precipitation, and column chromatography on Sephadex G-150, CM Sephadex C-50 and DEAE Sephadex A-50. This gave milk-activator with a maximum purification factor of about 2,400-fold with respect to the skimmed milk. The CM Sephadex-step preparation showed, on polyacrylamide gel electrophoresis, a single plasminogen-activator activity band located between the bands of albumin and prealbumin of human serum. This preparation exhibited no kinin forming activity. The activator hydrolyzed acetyl-glycyl-L-lysine methyl ester with similar order kinetic constants to urokinase, and was inhibited strongly by diisopropyl-fluorophosphate. The molecular weight of the activator as estimated by gel filtration was approximately 86,000, the isoelectric points as estimated by gel isoelectric focusing were pH 7.2, 6.9 and 6.6, and the activator activity was not quenched by antiurokinase globulin, indicating that the milk-activator is a different entity from urokinase.

Keywords

Plasminogen-activator - Milk-activator - Fibrinolysis
 

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