Use of a phosphopeptide as a ligand to purify phospholipase A2 from the venom of Crotalus durisuss terrificus by affinity chromatography

2020 ◽  
Vol 1146 ◽  
pp. 122070 ◽  
Author(s):  
Soledad L. Saavedra ◽  
Gerardo Acosta ◽  
Lucía Ávila ◽  
Silvana L. Giudicessi ◽  
Silvia A. Camperi ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Affinity Chromatography

Affinity chromatography of phospholipase A2 from Naja naja naja (Indian cobra) venom

Toxicon ◽  
1985 ◽  
Vol 23 (3) ◽  
pp. 457-466 ◽  
Author(s):  
Theodore L. Hazlett ◽  
Edward A. Dennis
Keyword(s):  
Phospholipase A2 ◽  
Affinity Chromatography ◽  
Cobra Venom ◽  
Naja Naja

The microstructure of functionalized poLyacrylonitrile beads for bioseparations

1990 ◽  
Vol 48 (4) ◽  
pp. 1094-1095
Author(s):  
Eduardo A. Kamenetzky ◽  
David A. Ley
Keyword(s):  
Aqueous Solution ◽  
Affinity Chromatography ◽  
Pore Size Distribution ◽  
Pore Size ◽  
Surface Coverage ◽  
Vacuum Impregnation ◽  
Thin Sections ◽  
Selective Staining ◽  
Low Viscosity ◽  
Diamond Knife

The microstructure of polyacrylonitrile (PAN) beads for affinity chromatography bioseparations was studied by TEM of stained ultramicrotomed thin-sections. Microstructural aspects such as overall pore size distribution, the distribution of pores within the beads, and surface coverage of functionalized beads affect performance properties. Stereological methods are used to quantify the internal structure of these chromatographic supports. Details of the process for making the PAN beads are given elsewhere. TEM specimens were obtained by vacuum impregnation with a low-viscosity epoxy and sectioning with a diamond knife. The beads can be observed unstained. However, different surface functionalities can be made evident by selective staining. Amide surface coverage was studied by staining in vapor of a 0.5.% RuO4 aqueous solution for 1 h. RuO4 does not stain PAN but stains, amongst many others, polymers containing an amide moiety.

Deficiency of Group VIA phospholipase A2 Primes the Cytokine Releases by Kupffer cells and Lymphocytes

2015 ◽  
Vol 53 (12) ◽  
Author(s):  
J Inhoffen ◽  
S Tuma-Kellner ◽  
W Stremmel ◽  
W Chamulitrat
Keyword(s):  
Phospholipase A2 ◽  
Kupffer Cells

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

Sign in / Sign up

Export Citation Format

Share Document