scholarly journals A tandem Kunitz protease inhibitor (KPI106)-serine carboxypeptidase (SCP1) controls mycorrhiza establishment and arbuscule development inMedicago truncatula

2013 ◽  
Vol 75 (5) ◽  
pp. 711-725 ◽  
Author(s):  
Stefanie S. Rech ◽  
Sven Heidt ◽  
Natalia Requena
Keyword(s):  
Protease Inhibitor ◽  
Serine Carboxypeptidase ◽  
Kunitz Protease Inhibitor

P4-153: The disruption of A-Beta peptide by transthyretin: A mechanism sensitive to Kunitz Protease Inhibitor

2009 ◽  
Vol 5 (4S_Part_16) ◽  
pp. P476-P476
Author(s):  
Rita Costa ◽  
Frederico Ferreira-da Silva ◽  
Maria Joao Saraiva ◽  
Isabel Cardoso
Keyword(s):  
Protease Inhibitor ◽  
Kunitz Protease Inhibitor ◽  
Beta Peptide

scholarly journals Tubers from potato lines expressing a tomato Kunitz protease inhibitor are substantially equivalent to parental and transgenic controls

2010 ◽  
Vol 8 (2) ◽  
pp. 155-169 ◽  
Author(s):  
Moustafa Khalf ◽  
Charles Goulet ◽  
Juan Vorster ◽  
France Brunelle ◽  
Raphaël Anguenot ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Kunitz Protease Inhibitor

Recombinant kunitz protease inhibitor ameliorates reperfusion injury in rat lung transplantation

1998 ◽  
Vol 66 (2) ◽  
pp. 351-355 ◽  
Author(s):  
Itaru Nagahiro ◽  
Tyler White ◽  
Motoki Yano ◽  
Carlos H.R. Boasquevisque ◽  
Masafumi Hiratsuka ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Lung Transplantation ◽  
Reperfusion Injury ◽  
Rat Lung ◽  
Kunitz Protease Inhibitor

scholarly journals Investigation of a Potential Scintigraphic Tracer for Imaging Apoptosis: Radioiodinated Annexin V-Kunitz Protease Inhibitor Fusion Protein

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Mei-Hsiu Liao ◽  
Tong-Rong Jan ◽  
Chao-Chih Chiang ◽  
Kuo-Chen Yen ◽  
Tse-Zung Liao ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protease Inhibitor ◽  
Annexin V ◽  
High Yield ◽  
Apoptotic Cells ◽  
Erythrocyte Ghosts ◽  
Kunitz Protease Inhibitor ◽  
Apoptosis Detection ◽  
Iodine 123 ◽  
Iodine 125

Radiolabeled annexin V (ANV) has been widely used for imaging cell apoptosis. Recently, a novel ANV-Kunitz-type protease inhibitor fusion protein, ANV-6L15, was found to be a promising probe for improved apoptosis detection based on its higher affinity to phosphatidylserine (PS) compared to native ANV. The present paper investigates the feasibility of apoptosis detection using radioiodinated ANV-6L15. Native ANV and ANV-6L15 were labeled with iodine-123 and iodine-125 using Iodogen method. The binding between the radioiodinated proteins and erythrocyte ghosts or chemical-induced apoptotic cells was examined. ANV-6L15 can be radioiodinated with high yield (40%−60%) and excellent radiochemical purity (>95%).123I-ANV-6L15 exhibited a higher binding ratio to erythrocyte ghosts and apoptotic cells compared to123I-ANV. The biodistribution of123I-ANV-6L15 in mice was also characterized.123I-ANV-6L15 was rapidly cleared from the blood. High uptake in the liver and the kidneys may limit the evaluation of apoptosis in abdominal regions. Our data suggest that radiolabled ANV-6L15 may be a better scintigraphic tracer than native ANV for apoptosis detection.

A genetically engineered human Kunitz protease inhibitor with increased kallikrein inhibition in an ovine model of cardiopulmonary bypass

Perfusion ◽  
2001 ◽  
Vol 16 (3) ◽  
pp. 199-206 ◽  
Author(s):  
Sunil K Ohri ◽  
Rachel Parratt ◽  
Tyler White ◽  
Jenny Becket ◽  
John J Brannan ◽  
...  
Keyword(s):  
Cardiopulmonary Bypass ◽  
Protease Inhibitor ◽  
Randomized Study ◽  
Genetically Engineered ◽  
Wild Type ◽  
Ovine Model ◽  
Double Blind ◽  
Perioperative Bleeding ◽  
Kunitz Inhibitor ◽  
Kunitz Protease Inhibitor

A recombinant human serine protease inhibitor known as Kunitz protease inhibitor (KPI) wild type has functional similarities to the bovine Kunitz inhibitor, aprotinin, and had shown a potential to reduce bleeding in an ovine model of cardiopulmonary bypass (CPB). The aim of this study was to assess KPI-185, a modification of KPI-wild type that differs from KPI-wild type in two amino acid residues and which enhances anti-kallikrein activity in a further double-blind, randomized study in an ovine model of CPB, and to compare with our previous study of KPI-wild type and aprotinin in the same ovine model. Post-operative drain losses and subjective assessment of wound ‘dryness’ showed no significant differences between KPI-185 and KPI-wild type, despite the significant enhancement of kallikrein inhibition using KPI-185 seen in serial kallikrein inhibition assays. These preliminary findings support the hypothesis that kallikrein inhibition is not the major mechanism by which Kunitz inhibitors such as aprotinin reduce perioperative bleeding.

scholarly journals Identification of a filamentous form of kunitz protease inhibitor in Asteraceae

2021 ◽  
Author(s):  
Sara Bratsch ◽  
Neil Olszewski ◽  
Benham Lockhart
Keyword(s):  
Protease Inhibitor ◽  
Protein Sequencing ◽  
Major Protein ◽  
Kunitz Trypsin Inhibitor ◽  
Terminal Protein ◽  
Filamentous Form ◽  
First Report ◽  
Kunitz Protease Inhibitor ◽  
Sds Page ◽  
Filament Protein

AbstractFilamentous structures were observed in purified extracts from chrysanthemum, gerbera, sunflower and zinnia. When purified filament proteins were subjected to SDS-PAGE, the major protein associated with filaments from all three species has an apparent molecular mass of ≈25 kDa. Protein bands from chrysanthemum, gerbera, and zinnia were subjected to N-terminal protein sequencing while proteins from sunflower were sequenced by CID MS/MS. All of the sequences shared highest similarity to the kunitz trypsin inhibitor family. The sequencing results indicated that the proteins lacked the signal sequences. We tested the gerbera filament protein for glycosylation and found that it was a glycoprotein. Together these results indicate that the filaments are composed of mature KTI protein. This is the first report of a KTI assembling into filaments and the first report of a filament forming Asteraceae enzyme.

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