Purification and biochemical properties of human plasminogen.
نویسندگان
چکیده
Plasminogen is the plasma precursor of the fibrinolytic enzyme, plasmin. The activation of plasminogen isolated from various animal species by streptokinase, a protein of bacterial origin, has received considerable attention in recent years. A two-step reaction has been postulated wherein streptokmase reacts with a substance termed proactivator (1)) which is present in highest concentration in human plasma and human plasminogen preparations and apparently is absent from the plasma of certain animal species such as the cow, to form an activator of human plasminogen (2) and the plasminogens of other animal species (3). The existence of proactivator as an entity distinct from human plasminogen is still hypothetical, since it has not been isolated in pure form. In fact, evidence has been presented (4, 5) which indicates that proactivator is human plasminogen. The purpose of this study was to attempt to isolate proactivator in pure form. Column chromatography of human plasminogen, prepared by the method of Kline (6), on carboxymethyl cellulose, has resulted in a 2to 4-fold purification. Although a high degree of homogeneity is apparent from physicochemical (7) and serological data, chromatographed plasminogen still retains essentially the same ratio of proactivator activity to plasminogen activity as that in crude preparations. The results of these studies are therefore interpreted as further evidence for the identity of proactivator and human plasminogen.
منابع مشابه
Preparation of Plasminogen by Affinity Chromatography
Background: Plasminogen is one of the compounds derived from human plasma. Activation of plasminogen produces plasmin. Plasmin is able to lyse fibrinogen, fibrin, and some other human plasma proteins. The aim of the present work was to study the separation of human plasminogen by affinity chromatography using gel lysine Sepharose. Materials and Methods: Normal human plasma was used as the...
متن کاملPurification and characterization of single-chain urokinase-type plasminogen activator from human cell cultures.
A urokinase-type plasminogen activator was purified from conditioned media of several human cell cultures, but preferably from the human lung adenocarcinoma line CALU-3 (ATCC, HTB-55), using a combination of chromatography on zinc chelate-Sepharose, SP-Sephadex C-50, and Sephadex G-100. Final yields of 65-100 micrograms/liter of starting material were obtained with a 290-fold purification facto...
متن کاملPurification and biochemical properties of a thermostable, haloalkaline cellulase from Bacillus licheniformis AMF-07 and its application for hydrolysis of different cellulosic substrates to bioethanol production
A thermophilic strain AMF-07, hydrolyzing carboxymethylcellulose (CMC) was isolated from Kerman hot spring and was identified as Bacillus licheniformis based on 16S rRNA sequence homology. The carboxymethylcellulase (CMCase) enzyme produced by the B. licheniformis was purified by (NH4)2SO4 precipitation, ion exchange and gel filtration chromatography. The purified enzyme gave a single band on S...
متن کاملPartial purification and properties of a proteolytic enzyme of human serum.
PARTIAL PURIFICATION AND PROPERTIES OF A PROTEOLYTIC ENZYME OF HUMAN SERUM. L. F. Remmert and P. P. Cohen. From the Laboratory of Physiological Chemistry, University of Wisconsin, Madison, Wis. J. Biol. Chem. i8i.’ 431-448, 1949. A method of partial purification of plasminogen is described and the suggestion is made that human serum contains only one proteolytic enzyme that is activated by stre...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of biological chemistry
دوره 235 شماره
صفحات -
تاریخ انتشار 1960