scholarly journals Conservative mutation met8 → leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I

2008 ◽  
Vol 9 (2) ◽  
pp. 273-279 ◽  
Author(s):  
Igor Zhukov ◽  
Andrzej Bierzynaski ◽  
Lukasz Jaroszewski
Keyword(s):  
Structural Stability ◽  
Trypsin Inhibitor ◽  
Folding Process ◽  
Squash Trypsin Inhibitor

Solution Structure of the Squash Trypsin Inhibitor MCoTI-II. A New Family for Cyclic Knottins†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (27) ◽  
pp. 7973-7983 ◽  
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
T. Trân Châu Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination

2002 ◽  
Vol 58 (9) ◽  
pp. 1448-1461 ◽  
Author(s):  
Ram Thaimattam ◽  
Ewa Tykarska ◽  
Andrzej Bierzynski ◽  
George M. Sheldrick ◽  
Mariusz Jaskolski
Keyword(s):  
Trypsin Inhibitor ◽  
Atomic Resolution ◽  
Metal Coordination ◽  
Squash Trypsin Inhibitor ◽  
Resolution Structure

scholarly journals Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

2010 ◽  
Vol 22 (2) ◽  
pp. 73-79 ◽  
Author(s):  
Leonardo A Calderon ◽  
Humberto A Almeida Filho ◽  
Rozeni C. L Teles ◽  
Francisco J Medrano ◽  
Carlos Bloch Jr ◽  
...  
Keyword(s):  
Structural Stability ◽  
Trypsin Inhibitor

Solution Structure of the Macrocyclic Squash Trypsin Inhibitor MCoTI-II, the First Member of a New Family of Cyclic Knottins

2001 ◽  
pp. 387-388
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
Châu T. T. Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

scholarly journals The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin.

1996 ◽  
Vol 43 (3) ◽  
pp. 503-506 ◽  
Author(s):  
W Watorek ◽  
A Polanowski ◽  
T Wilusz
Keyword(s):  
Affinity Chromatography ◽  
Trypsin Inhibitor ◽  
Efficient Method ◽  
Human Neutrophil ◽  
Cathepsin G ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Human Neutrophils ◽  
Human Neutrophil Elastase ◽  
Pancreatic Trypsin Inhibitor ◽  
Squash Trypsin Inhibitor

Elastase, cathepsin G and azurocidin from human neutrophils are key components of body inflammatory defense. Perturbations in regulation of their activities lead to many serious pathological states. The paper describes a simple, fast and efficient method of joint purification of these proteins with the use of sequential affinity chromatography on squash trypsin inhibitor (CMTI I) and bovine pancreatic trypsin inhibitor (BPTI).

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