scholarly journals Affinity Chromatography as a Key Tool to Purify Protein Protease Inhibitors from Plants

10.5772/34982 ◽  
2012 ◽  
Author(s):  
Elizeu Antunes dos Santos ◽  
Adeliana Silva de Oliveira ◽  
Luciana Maria Arajo Rablo ◽  
Adriana Ferreira ◽  
Ana Heloneida Arajo Morais
Keyword(s):  
Affinity Chromatography ◽  
Protease Inhibitors

HSA binding of HIV protease inhibitors: a high-performance affinity chromatography study

2009 ◽  
Vol 32 (10) ◽  
pp. 1625-1631 ◽  
Author(s):  
Carlo Bertucci ◽  
Marco Pistolozzi ◽  
Guy Felix ◽  
U. Helena Danielson
Keyword(s):  
Affinity Chromatography ◽  
Protease Inhibitors ◽  
High Performance ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
High Performance Affinity Chromatography

scholarly journals Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae

2014 ◽  
Vol 23 (2) ◽  
pp. 187-193 ◽  
Author(s):  
Sedigheh Nabian ◽  
Mohammad Taheri ◽  
Mohammad Mehdi Ranjbar ◽  
Alireza Sazmand ◽  
Parastou Youssefy ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Serine Protease ◽  
Protease Inhibitors ◽  
Inflammatory Responses ◽  
Blood Feeding ◽  
Immune Serum ◽  
Partial Purification ◽  
Hard Tick ◽  
Two Dimensional ◽  
Serine Protease Inhibitors

Ticks are rich sources of serine protease inhibitors, particularly those that prevent blood clotting and inflammatory responses during blood feeding. The tick Rhipicephalus (Boophlus) annulatusis an important ectoparasite of cattle. The aims of this study were to characterize and purify the serine protease inhibitors present in R. (B.) annulatus larval extract. The inhibitors were characterized by means of one and two-dimensional reverse zymography, and purified using affinity chromatography on a trypsin-Sepharose column. The analysis on one and two-dimensional reverse zymography of the larval extract showed trypsin inhibitory activity at between 13 and 40 kDa. Through non-reducing SDS-PAGE and reverse zymography for proteins purified by trypsin-Sepharose affinity chromatography, some protein bands with molecular weights between 13 and 34 kDa were detected. Western blotting showed that five protein bands at 48, 70, 110, 130 and 250 kDa reacted positively with immune serum, whereas there was no positive reaction in the range of 13-40 kDa. Serine protease inhibitors from R. (B.) annulatus have anti-trypsin activity similar to inhibitors belonging to several other hard tick species, thus suggesting that these proteins may be useful as targets in anti-tick vaccines.

scholarly journals The Value of Fungal Protease Inhibitors in Affinity Chromatography

10.5772/35354 ◽  
2012 ◽  
Author(s):  
Jerica Saboti ◽  
Katarina Koruza ◽  
Botjan Gabor ◽  
Matja Peterka ◽  
Milo Barut ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Protease Inhibitors ◽  
Fungal Protease

SEM of non-coated hepatocellular cytoskeleton of perfused livers

1984 ◽  
Vol 42 ◽  
pp. 306-307
Author(s):  
S.W. French ◽  
N.C. Benson ◽  
C. Davis-Scibienski
Keyword(s):  
Ambient Temperature ◽  
Critical Point ◽  
Protease Inhibitors ◽  
Metal Deposition ◽  
Heat Damage ◽  
Detergent Extraction ◽  
Cytoskeletal Elements ◽  
Triton X ◽  
Excised Tissue

Previous SEM studies of liver cytoskeletal elements have encountered technical difficulties such as variable metal coating and heat damage which occurs during metal deposition. The majority of studies involving evaluation of the cell cytoskeleton have been limited to cells which could be isolated, maintained in culture as a monolayer and thus easily extracted. Detergent extraction of excised tissue by immersion has often been unsatisfactory beyond the depth of several cells. These disadvantages have been avoided in the present study. Whole C3H mouse livers were perfused in situ with 0.5% Triton X-100 in a modified Jahn's buffer including protease inhibitors. Perfusion was continued for 1 to 2 hours at ambient temperature. The liver was then perfused with a 2% buffered gluteraldehyde solution. Liver samples including spontaneous tumors were then maintained in buffered gluteraldehyde for 2 hours. Samples were processed for SEM and TEM using the modified thicarbohydrazide procedure of Malich and Wilson, cryofractured, and critical point dried (CPD). Some samples were mechanically fractured after CPD.

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.

Protease inhibitors vindicated in 1997

1998 ◽  
Vol 6 (11) ◽  
pp. 174
Keyword(s):  
Protease Inhibitors
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