ライフサイエンスコーパス: caseinolytic

1 lagenolytic, gelatinolytic, elastolytic, and caseinolytic activities in vivo by the transduced fibrob

2 n batch mode, by evaluating protein loading, caseinolytic activity and the coagulation properties of

3 and substrate conditions using esterase and caseinolytic activity assays and time course hydrolysis

4 olytic activity at 92 and 72 kDa, as well as caseinolytic activity at 57, 45, and 19 kDa in the lipid

5 HT had the highest rate of caseinolytic activity at the lowest concentration (0.1 m

6 onal antibodies against proteinase 3 removed caseinolytic activity from wound fluid, and that purifie

7 Caseinolytic activity in wound fluid increased markedly

8 In this study, we analyzed caseinolytic activity in wound fluid obtained from acute

9 Weak caseinolytic activity inhibitable by cysteine protease i

10 gs suggested that the enzyme responsible for caseinolytic activity might be proteinase 3, an elastase

11 Val was a reasonably potent inhibitor of the caseinolytic activity of 20 S proteasome, producing 50%

12 alytic Cys residue to Ser leads to a loss of caseinolytic activity of DEK1 domain II&III.

13 There was increased caseinolytic activity of MMP-3 and collagenolytic activi

14 tone produced half-maximum inhibition of the caseinolytic activity of mu-calpain at concentrations of

15 Caseinolytic activity of the precipitated protein fracti

16 on, as determined both by immunoblotting and caseinolytic activity on agar plates.

17 Highest caseinolytic activity on azocasein was detected after pr

18 tioned medium of these cultures (measured as caseinolytic activity) was enhanced by L-NMA; however, t

19 Abnormally high levels of caseinolytic activity, consistent with NE, were detected

20 ly expressed DEK1 domain II does not display caseinolytic activity, suggesting an important role for

21 artilage matrix loss with increased secreted caseinolytic activity.

22 0 mg mL(-1) to achieve their maximum rate of caseinolytic activity.

23 nzyme accounted for approximately 80% of the caseinolytic activity.

24 eports the detection and characterization of caseinolytic and milk-clotting activities from Moringa o

25 yperlipemic groups elaborated gelatinolytic, caseinolytic, and elastinolytic activity attributable to

26 A caseinolytic assay and Western blotting indicated that s

27 DEK1 domain II&III exhibits activity in the caseinolytic assay in the absence of calcium, although t

28 tructure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A r

29 due to a down-regulation of gelatinolytic or caseinolytic matrix metalloproteinases.

30 Whereas the plastid caseinolytic peptidase (Clp) P protease system is essent

31 y to HEAT SHOCK PROTEIN 101, which encodes a caseinolytic peptidase B chaperonin required for thermot

32 can, we identified biallelic variants in the caseinolytic peptidase B homolog (CLPB).

33 CLPB encodes caseinolytic peptidase B homolog ClpB, a member of the A

34 Caseinolytic peptidase P (ClpP), a double-ring peptidase

35 and that purified proteinase 3 had a similar caseinolytic profile and inhibitor sensitivity to burn f

36 The caseinolytic protease (Clp) protease system has been exp

37 Here, we show that the caseinolytic protease (Clp) substrate adaptor ClpS1 and

38 Plants defective in the chloroplast caseinolytic protease (Clp) system were specifically imp

39 ial agents that act through dysregulation of caseinolytic protease (ClpP).

40 s thaliana), the At1g74310 locus encodes for caseinolytic protease B-cytoplasmic (ClpB-C)/heat shock

41 to 10-fold up-regulation of AtRH3 in plastid Caseinolytic protease mutants.

42 The barrel-shaped caseinolytic protease P (ClpP) is a main virulence regul

43 Caseinolytic protease P (ClpP) represents a central bact

44 recombination system we have deleted clpP1 (caseinolytic protease P1), one of the three genes (clpP1

45 A well-conserved protein complex named ClpP (caseinolytic protease) plays a vital role in adaptation

46 The ATP-dependent caseinolytic protease, ClpP, is highly conserved in bact

47 Caseinolytic proteases (ClpPs) are large oligomeric prot

48 ined for the expression of gelatinolytic and caseinolytic proteases as well as for proteinase inhibit