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

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

Properties of fungal protease inhibitors from the integument and haemolymph of the silkworm and effect of an inhibitor on the fungal growth

1990 ◽  
Vol 95 (3) ◽  
pp. 559-564 ◽  
Author(s):  
Susumu Yoshida ◽  
Masaki Yamashita ◽  
Satoshi Yonehara ◽  
Masaharu Eguchi
Keyword(s):  
Protease Inhibitors ◽  
Fungal Growth ◽  
Fungal Protease

scholarly journals Microbial and fungal protease inhibitors—current and potential applications

2012 ◽  
Vol 93 (4) ◽  
pp. 1351-1375 ◽  
Author(s):  
Jerica Sabotič ◽  
Janko Kos
Keyword(s):  
Protease Inhibitors ◽  
Potential Applications ◽  
Fungal Protease

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.

Fungal Protease Inhibitors

2015 ◽  
pp. 1-33
Author(s):  
Jerica Sabotič ◽  
Janko Kos
Keyword(s):  
Protease Inhibitors ◽  
Fungal Protease

Fungal Protease Inhibitors

2017 ◽  
pp. 853-885
Author(s):  
Jerica Sabotič ◽  
Janko Kos
Keyword(s):  
Protease Inhibitors ◽  
Fungal Protease

Genetic variants of protease inhibitors against fungal protease and ?-chymotrypsin from hemolymph of the silkworm, Bombyx mori

1984 ◽  
Vol 22 (11-12) ◽  
pp. 1093-1102 ◽  
Author(s):  
M. Eguchi ◽  
K. Ueda ◽  
M. Yamashita
Keyword(s):  
Bombyx Mori ◽  
Protease Inhibitors ◽  
Genetic Variants ◽  
Fungal Protease ◽  
Silkworm Bombyx Mori
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