scholarly journals Reduction and carboxamidomethylation of the single disulfide bond of proteinase inhibitor I from potato tubers. Effects on stability, immunological properties, and inhibitory activities.

1980 ◽  
Vol 255 (7) ◽  
pp. 2752-2755
Author(s):  
G. Plunkett ◽  
C.A. Ryan
Keyword(s):  
Disulfide Bond ◽  
Proteinase Inhibitor ◽  
Potato Tubers ◽  
Immunological Properties ◽  
Inhibitory Activities

Synthesis of the proteinase inhibitor LEKTI domain 6 by the fragment condensation method and regioselective disulfide bond formation

Biopolymers ◽  
2010 ◽  
Vol 94 (3) ◽  
pp. 339-349 ◽  
Author(s):  
Zoe Vasileiou ◽  
Kostas K. Barlos ◽  
Dimitrios Gatos ◽  
Knut Adermann ◽  
Celine Deraison ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Proteinase Inhibitor ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Condensation Method ◽  
Fragment Condensation

Variability in the concentration of three heat stable proteinase inhibitor proteins in potato tubers

1976 ◽  
Vol 53 (12) ◽  
pp. 443-455 ◽  
Author(s):  
C. A. Ryan ◽  
T. Kuo ◽  
G. Pearce ◽  
R. Kunkel
Keyword(s):  
Proteinase Inhibitor ◽  
Potato Tubers ◽  
Heat Stable

Immunocytochemical Intracellular Localization of the 22-ku Kunitz-type Potato Proteinase Inhibitor in Potato Tubers and Leaves

1999 ◽  
Vol 155 (4-5) ◽  
pp. 533-537
Author(s):  
Sang-Gon Suh ◽  
Jun-Koo Cho ◽  
Eun-Jung Suh ◽  
Hee-Don Chung ◽  
David J. Hannapel
Keyword(s):  
Proteinase Inhibitor ◽  
Intracellular Localization ◽  
Potato Tubers ◽  
Kunitz Type

scholarly journals The effect of synthetic analogues of chymostatin upon protein degradation in isolated skeletal muscle

1985 ◽  
Vol 229 (2) ◽  
pp. 491-497 ◽  
Author(s):  
M T Mulligan ◽  
I J Galpin ◽  
A H Wilby ◽  
R J Beynon
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Lactate Dehydrogenase ◽  
Protein Degradation ◽  
Incubation Medium ◽  
Proteinase Inhibitor ◽  
Structural Features ◽  
Marked Contrast ◽  
Significant Toxicity ◽  
Inhibitory Activities

A series of peptides based on the structure of the proteinase inhibitor chymostatin were tested for their toxicity and ability to suppress protein degradation in the isolated mouse diaphragm. The inhibitory activities of the analogues were very similar, in marked contrast to their disparate abilities as inhibitors of chymotrypsin. Toxicity was determined by measurement of the rates of protein synthesis and of leakage of lactate dehydrogenase into the incubation medium. No significant toxicity was measurable at concentrations of inhibitor that were effective at suppressing proteolysis. The structural features of the chymostatin molecule may be less than optimal for suppression of proteolysis in muscle.

scholarly journals Gene Expression of a Kunitz-type Proteinase Inhibitor and Patatin in Response to Storage Temperature of Potato Tubers.

1994 ◽  
Vol 63 (2) ◽  
pp. 368-369
Author(s):  
Kazutoshi YAMAGISHI ◽  
Koh NAGATANI ◽  
Takako TUKASE ◽  
Cristina MITSUMORI ◽  
Eliza Mitiko ISEJIMA ◽  
...  
Keyword(s):  
Gene Expression ◽  
Proteinase Inhibitor ◽  
Storage Temperature ◽  
Potato Tubers ◽  
Kunitz Type

scholarly journals Nucleotide and deduced amino acid sequence of an aspartic proteinase inhibitor homologue from potato tubers (Solanum tuberosum L.)

1990 ◽  
Vol 18 (15) ◽  
pp. 4605-4605 ◽  
Author(s):  
B. Strukelj ◽  
J. Pungercar ◽  
A. Ritonja ◽  
I. Krizaj ◽  
F. Gubensek ◽  
...  
Keyword(s):  
Solanum Tuberosum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteinase Inhibitor ◽  
Solanum Tuberosum L ◽  
Aspartic Proteinase ◽  
Potato Tubers
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