Stimulation of enzymatic activity in filament preparations of casein kinase II by polylysine, melittin, and spermine

1989 ◽  
Vol 85 (2) ◽  
pp. 147-157 ◽  
Author(s):  
Mark D. Mamrack
Keyword(s):  
Enzymatic Activity ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Stimulation Of

scholarly journals A polylysine-induced aggregation of substrate accompanies the stimulation of casein kinase II by polylysine

1993 ◽  
Vol 289 (3) ◽  
pp. 631-635 ◽  
Author(s):  
F J Moreno ◽  
C G Lechuga ◽  
M Collado ◽  
M J Benítez ◽  
J S Jiménez
Keyword(s):  
Electron Microscopy ◽  
Concentration Dependence ◽  
Gel Filtration ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Preliminary Results ◽  
Enzyme Stimulation ◽  
Induced Aggregation ◽  
Basic Polypeptides ◽  
Stimulation Of

Casein kinase II (CK-II) activation by polylysine parallels an aggregation of substrates promoted by the polycation. CK-II is known to be stimulated by basic polypeptides and polyamines. The mechanism by which this stimulation takes place, however, is not yet fully understood. Here we show that, in the usual CK-II assay, polylysine induces the aggregation of casein. This aggregation has been monitored by turbidimetry, electron microscopy and gel filtration. The polylysine-concentration-dependence of the casein aggregation parallels the polylysine-concentration-dependence of the enzyme stimulation. In the presence of polylysine the enzyme is incorporated into the casein aggregates promoted by the polycation, thus supporting the view that this substrate aggregation is directly related to the mechanism of CK-II stimulation. Preliminary results show that a similar parallelism occurs with other natural substrates of the enzyme. The physiological meaning of this substrate aggregation, and its possible relation to other polylysine-stimulated enzymes and polylysine-aggregated proteins, are discussed.

Synergistic stimulation of fibrinogen gelation by casein kinase II and polycationic compounds

IUBMB Life ◽  
1997 ◽  
Vol 42 (3) ◽  
pp. 487-495 ◽  
Author(s):  
Kyoungho Suk ◽  
Jin-Young Lee ◽  
Seung-Ho Kim
Keyword(s):  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Stimulation Of

Isolation of Antithrombin III from Normal and α1-Antitrypsin-Deficient Human Plasma

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Antithrombin Activity ◽  
Bovine Trypsin ◽  
Normal Plasma ◽  
Antitrypsin Deficiency ◽  
Simplified Procedure ◽  
Stimulation Of

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.

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