ライフサイエンスコーパス: heparin-agarose

1 84, R487, and K532 showed partial binding to heparin-agarose.

2 at position 585 or 588 eliminated binding to heparin-agarose.

3 sted for their ability to bind heparin using heparin-agarose affinity chromatography (HAAC).

4 eletal muscle laminins partially purified by heparin-agarose affinity chromatography also bound alpha

5 om both RSV subgroups A and B were tested by heparin-agarose affinity chromatography for their abilit

6 ycan (GAG) interactions were evaluated using heparin-agarose affinity chromatography.

7 ectin was removed from fetal bovine serum by heparin-agarose affinity chromatography.

8 plexing the latter with thrombin followed by heparin-agarose affinity chromatography.

9 s separated into two major enzyme species by heparin-agarose affinity chromatography.

10 contains an EGF-like mitogen that binds to a heparin-agarose affinity matrix with high affinity.

11 fold from calf brain using chromatography on heparin-agarose and affinity elution with inositol hexak

12 ymerase from growing M. xanthus cells, using heparin-agarose and DNA-cellulose chromatographies.

13 lls, and the recombinant protein purified by heparin-agarose and gel-filtration chromatography.

14 y chromatography on DE-23, phenyl-Sepharose, heparin-agarose, and butyl-Sepharose.

15 d to apparent homogeneity by DEAE-cellulose, heparin-agarose, and DNA-specific affinity chromatograph

16 ography on DEAE-cellulose, phosphocellulose, heparin-agarose, and single-stranded DNA-cellulose.

17 chromatography that hIL-10 binds strongly to heparin-agarose at physiological pH.

18 WG also binds directly to heparin agarose beads with high affinity.

19 d TRSB and TRSB-R114 attached efficiently to heparin-agarose beads in binding assays, while TR339 sho

20 achment to cells and efficient attachment to heparin-agarose beads, presumably because the furin reco

21 deletion was capable of efficient binding to heparin-agarose beads, suggesting different requirements

22 The DeltaTMgpK8.1A specifically bound to heparin-agarose beads, which was inhibited by HS and hep

23 ted gpK8.1A was specifically precipitated by heparin-agarose beads.

24 inity binding to BHK cells and attachment to heparin-agarose beads.

25 ons R585 and R588 to lysine slightly reduced heparin-agarose binding and had comparable effects on in

26 We observed a general correlation between heparin-agarose binding and infectivity as measured by G

27 y ammonium sulfate precipitation followed by heparin agarose chromatography.

28 m sulphate precipitation, octyl agarose, and heparin agarose chromatography.

29 purified by ammonium-sulphate precipitation, heparin-agarose chromatography and gel filtration.

30 solution of delta helicase from pol delta on heparin-agarose chromatography and its purification to a

31 tis RNA polymerase was partially purified by heparin-agarose chromatography and used in conjunction w

32 However, by heparin-agarose chromatography of high-salt extracts of

33 relatent antithrombin that are resolvable by heparin-agarose chromatography.

34 rotein is separable from the PLD activity by heparin-agarose chromatography.

35 ations sufficient to elute prochymase from a heparin agarose column.

36 AAV5 generated a hybrid virus that bound to heparin-agarose efficiently and was able to package DNA

37 GE1, P123/GE1, and CP123/GE1 bound poorly to heparin-agarose except in the absence of sodium chloride

38 peptide beta 15-42 showed highest binding to heparin-agarose followed by B beta 1-42, whereas peptide

39 125I-LDL bound to HL-saturated heparin-agarose gel with a Kd of 52 nM, and somewhat sur

40 NaCl-solubilized HIP bound to heparin-agarose in physiological saline and eluted with

41 ds were assayed for their ability to bind to heparin-agarose in vitro, and virions that packaged DNA

42 ferent columns (DEAE-Sepharose, Econo S, and heparin-agarose), LRP was primarily associated with cdk2

43 let CKII kinase was partially purified using heparin-agarose, phosphocellulose, and ion exchange chro

44 er, a subset of mutants that partially bound heparin-agarose (R484A and K532A) were completely noninf

45 inity enzyme forms that were not retained on heparin agarose showed strong crossreactivity in immunob

46 Binding of fibrin(ogen) to heparin agarose was saturable as well as inhibitable in

47 Elution from heparin-agarose with a linear gradient of NaCl showed th