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bowman birk inhibitor/soja warzywna

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Ultrastructural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soybean) cv. Maple Arrow by the gold method.

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The soybean Bowman-Birk inhibitor (BBI), a polypeptide of MW 8,000, has a specificity directed against trypsin and chymotrypsin. BBI was localized at the ultrastructural level by the protein A gold method on thin sections of Glycine max (soybean) cv. Maple Arrow. In cotyledon and embryonic axis, BBI
Pancreatic weights and composition were studied with rats fed diets containing raw legume seeds for up to 800 d. Rapid pancreatic enlargement was induced by dietary soybeans (Glycine max) (high Kunitz and Bowman-Birk trypsin inhibitor contents, moderate lectin content) during the initial 150 d. Over
Feeding trials have been done with rats to assess the effects of long-term (700 d) consumption of diets based on raw cowpeas (Vigna unguiculata; moderate Bowman-Birk inhibitor content, low lectin content), lupin seeds (Lupinus angustifolius; low lectin and protease inhibitor content) or soya beans

Bowman-Birk inhibitors, proteasome peptidase activities and colorectal pre neoplasias induced by 1,2-dimethylhydrazine in Swiss mice.

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Bowman-Birk inhibitors (BBIs) are protein molecules containing two inhibitory domains for enzymes similar to trypsin and chymotrypsin. Interest in these inhibitors arose from their properties against the cancer chemically induced by 1,2-dimethylhydrazine (DMH). In this study the effect of two BBI

Dermatological and cosmeceutical benefits of Glycine max (soybean) and its active components.

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Glycine max, known as the soybean or soya bean, is a species of legume native to East Asia. Soya beans contain many functional components including phenolic acids, flavonoids, isoflavonoids (quercetin, genistein, and daidzein), small proteins (Bowman-Birk inhibitor, soybean trypsin inhibitor)
Bowman-Birk inhibitors (BBI) from soybean and related proteins are naturally occurring protease inhibitors with potential health-promoting properties within the gastrointestinal tract. In this work, we have investigated the effects of soybean BBI proteins on HT29 colon adenocarcinoma cells, compared

[Cysteine proteinase inhibitors from soy seeds].

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Protein inhibitors of cysteine proteinases possessing unusual properties have been found in soya (Glycine max) seeds. One of the inhibitor forms has also been detected in Bowman-Birk inhibitor preparations (both commercial and purified by affinity chromatography on chymotrypsin-Sepharose ones). A

Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor, C-II.

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Soybean inhibitor C-II, which inhibits trypsin, alpha-chymotrypsin, and elastase, was reduced and S-carboxymethylated, and digested with trypsin. The amino acid sequences of the resulting tryptic peptides were determined by conventional methods, establishing the complete 76-amino acid sequence of

Different Rates of Metabolism of Soybean Proteinase Inhibitors during Germination.

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During germination, the content of the major Bowman-Birk proteinase inhibitor (BB-E) in the cotyledons of soybean (Glycine max [L.] Merrill cv. Fiskeby V) seeds decreases, becoming a minor form by the sixth day of germination. One of the three other minor species (BB-D) of this inhibitor in the dry

A Kunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on podborer (Helicoverpa armigera) larvae.

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Chickpea (Cicer arietinum L.) seeds contain Bowman-Birk proteinase inhibitors, which are ineffective against the digestive proteinases of larvae of the insect pest Helicoverpa armigera. We have identified and purified a low expressing proteinase inhibitor (PI), distinct from the Bowman-Birk

Immunoassays of soy proteins.

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Proteins of soybeans (Glycine max) are widely used in animal and human nutrition. In addition to the bulk of the seed storage proteins, which are classified as albumins and globulins, approximately 6% of soybean proteins are classified as inhibitors of trypsin and chymotrypsin and approximately 0.5%
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