Results 11 to 20 of about 3,419,991 (153)

CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR [PDF]

open access: yesJournal of General Physiology, 1947
A study has been made of the general properties of crystalline soybean trypsin inhibitor. The soy inhibitor is a stable protein of the globulin type of a molecular weight of about 24,000. Its isoelectric point is at pH 4.5.
Kunitz M
exaly   +6 more sources

Trypsin inhibitor from tamarindus indica L. seeds reduces weight gain and food consumption and increases plasmatic cholecystokinin levels

open access: yesClinics, 2015
OBJECTIVES: Seeds are excellent sources of proteinase inhibitors, some of which may have satietogenic and slimming actions. We evaluated the effect of a trypsin inhibitor from Tamarindus indica L.
Joycellane Alline do Nascimento Campos Ribeiro   +11 more
doaj   +2 more sources

Effects of infrared treatment on urease, trypsin inhibitor and lipoxygenase activities of soybean samples

open access: yesFood Chemistry, 2015
In this study, infrared (IR) treatment at different powers (814W, 1003W, 1208W, 1342W) and times (10min, 15min) were applied to unsoaked and soaked (30min, 45min) soybeans (cvs. Adasoy, Nazlican).
Arzu Basman
exaly   +2 more sources

Influence of Different Genotypes on Trypsin Inhibitor Levels and Activity in Soybeans

open access: yesSensors, 2007
This study describes the relationship between the two major trypsin inhibitors (TI) in soybean, i.e., the Kunitz (KTI) and Bowman-Birk (BBI) trypsin inhibitors, as well as between them and the corresponding trypsin inhibitor activity (TIA).
Viktor A. Nedovic   +4 more
doaj   +3 more sources

Pancreatic secretory trypsin inhibitor: More than a trypsin inhibitor.

open access: yesWorld Journal of Gastrointestinal Pathophysiology, 2010
Kazal-type serine protease inhibitor is one of the most important and widely distributed protease inhibitor families. Pancreatic secretory trypsin inhibitor (PSTI), also known as serine protease inhibitor Kazal type I(SPINK1), binds rapidly to trypsin ...
Gai-ping Wang, Cunshuan Xu
semanticscholar   +3 more sources

Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

open access: yesJournal of the American Oil Chemists' Society, 2021
AbstractFor expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement.
Keshun Liu
semanticscholar   +2 more sources

Adenanthera pavonina, a potential plant-based protein resource: Seed protein composition and immunohistochemical localization of trypsin inhibitors

open access: yesFood Chemistry: X, 2022
Adenanthera pavonina, an underutilized tropical tree, is being promoted as an alternative food source for meeting the nutritional needs of human and animals.
Hari B. Krishnan   +4 more
doaj   +1 more source

Insecticide activity of a peptidase inhibitor isolated from Anadenanthera macrocarpa seeds against Anagasta kuehniella

open access: yesCiência e Agrotecnologia, 2022
Protease inhibitors (PIs) are a part of the plant defense system and reduce the proteolytic activity of the digestive enzymes of insect pests. The current study aimed to isolate and characterize an inhibitor of trypsin (AmTI) within the seed of ...
Welington de Araújo Leite   +2 more
doaj   +1 more source

Multimeric Association of Purified Novel Bowman-Birk Inhibitor From the Medicinal Forage Legume Mucuna pruriens (L.) DC.

open access: yesFrontiers in Plant Science, 2021
A Bowman-Birk protease, i.e., Mucuna pruriens trypsin inhibitor (MPTI), was purified from the seeds by 55.702-fold and revealed a single trypsin inhibitor on a zymogram with a specific activity of 202.31 TIU/mg of protein.
Jafar K. Lone   +7 more
doaj   +1 more source

Conformational changes of rBTI from buckwheat upon binding to trypsin: implications for the role of the P(8)' residue in the potato inhibitor I family. [PDF]

open access: yesPLoS ONE, 2011
BWI-1 (buckwheat trypsin inhibitor), a member of the potato inhibitor I family, suppresses the growth of T-acute lymphoblastic leukemia cells and induces apoptosis in human solid tumor cell lines.
Longfei Wang   +8 more
doaj   +1 more source

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