By Laszlo Lorand

The severely acclaimed laboratory general, Methods in Enzymology, is among the so much hugely revered courses within the box of biochemistry. on account that 1955, every one quantity has been eagerly awaited, usually consulted, and praised via researchers and reviewers alike. The sequence comprises a lot fabric nonetheless suitable this present day - actually a necessary e-book for researchers in all fields of lifestyles sciences

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Acta 130, 92 (1966). 22y . Nemerson, J. Clin. Invest. 47, 72 (1968). 13y . Nemerson, ]. Clin. Invest. 48, 322 (1969). 24M. Hvatum, and H. Prydz, Thromb. Diath. Haemorrh. 21, 217 (1969). 38 BLOOD CLOTTING ENZYMES [5] protein can be solubilized with detergents and purified. While not all phospholipids reconstitute the active complex, certain phospholipids or mixture~ of phospholipids can be used interchangeably for reconstitution of the active lipoprotein. Preparation of Delipidated Tissue Powders Acetone Dehydration Bovine lung and other vascular tissues are homogenized in saline to remove serum proteins before acetone extraction; bovine brain is directly extracted with acetone.

A m m o n i u m sulfate precipitation. Filtration was used to remove material precipitated by 30% saturated a m m o n i u m sulfate, and centrifugation (20 min at 23,000 g) precipitated the tissue factor activity in 60% saturated ammonium sulfate. The protein solution was then absorbed onto and eluted from DEAE-Sephadex. More recently, we have found t h a t with centrifugation of both a m m o n i u m sulfate precipitation steps (1 hr at 23,000 g in a Beckman type 15 rotor), the specific activity of the tissue factor is the same as t h a t which has been eluted from DEAE-Sephadex.

16a Hirudin ~° provides an interesting biological example of anticoagulant proteins secreted by blood-sucking animals (see also Fritz and Krejci~l). Lysis of clots and the organization of thrombi is a complex event which p r o b a b l y involves the release of a number of intracellular enzymes. However, plasma also contains the precursor of a fibrinolytic enzyme, plasmin, 32,33 and this enzyme, too, belongs to the trypsin family of serine-OH proteases. Conversion of plasminogcn to plasmin can be brought about either by a direct hydrolytic a t t a c k by another protease, urokinase, 34 or indirectly through interaction with streptokinase 35 which, b y itself, displays no enzymic activity.

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