proteinase inhibitor/glycine max

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Role of cysteine proteinase inhibitors in preference of Japanese beetles (Popillia japonica) for soybean (Glycine max) leaves of different ages and grown under elevated CO2.

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Elevated levels of CO(2), equivalent to those projected to occur under global climate change scenarios, increase the susceptibility of soybean foliage to herbivores by down-regulating the expression of genes related to the defense hormones jasmonic acid and ethylene; these in turn decrease the gene

Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog.

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Diverse functions for three soybean (Glycine max L. Merr.) cysteine proteinase inhibitors (CysPIs) are inferred from unique characteristics of differential regulation of gene expression and inhibitory activities against specific Cys proteinases. Based on northern blot analyses, we found that the

[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

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 novel Glycine soja cysteine proteinase inhibitor GsCPI14, interacting with the calcium/calmodulin-binding receptor-like kinase GsCBRLK, regulated plant tolerance to alkali stress.

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It has been well demonstrated that cystatins regulated plant stress tolerance through inhibiting the cysteine proteinase activity under environmental stress. However, there was limited information about the role of cystatins in plant alkali stress response, especially in wild soybean. Here, in this

Insight into the biochemical characterization of phytocystatin from Glycine max and its interaction with Cd+2 and Ni+2.

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Phytocystatins are cysteine proteinase inhibitors ubiquitously present in plants and animals. They are known to carry out various significant physiological functions and also maintain the balance of protease-antiprotease activity. In the present disquisition, a phytocystatin after preliminary

Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate.

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Three cysteine proteinase inhibitor cDNA clones (pL1, pR1, and pN2) have been isolated from a soybean (Glycine max L. Merr.) embryo library. The proteins encoded by the clones are between 60 and 70% identical and contain the consensus QxVxG motif and W residue in the appropriate spatial context for

Multigene family for Bowman-Birk type proteinase inhibitors of wild soja and soybean: the presence of two BBI-A genes and pseudogenes.

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Genes for Bowman-Birk type protease inhibitors (BBIs) of wild soja (Glycine soja) and soybean (Glycine max) comprise a multigene family. The organization of the genes for wild soja BBIs (wBBIs) was elucidated by an analysis of their cDNAs and the corresponding genomic sequences, and compared with

Characterization of soybean endopeptidase activity using exogenous and endogenous substrates.

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Endopeptidase activity in mature soybean seeds (Glycine max), has been measured using an exogenous substrate, [(125)I]iodoinsulin B chain. On the basis of pH optimum and the use of specific proteinase inhibitors, two distinct endopeptidase activities can be identified in both the embryonic axis and

Subtilisin inhibitor like protein 'ppLPI-1' from leaves of pigeonpea (Cajanus cajan, cv. BSMR 736) exhibits inhibition against Helicoverpa armigera gut proteinases.

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Helicoverpa armigera is an orthodox rival of many crop plants affecting agricultural economy. Plant leaves found to accumulate proteinase inhibitors, although this insect pest chooses leaves for laying eggs. Plant defense response at this juncture is not fully explored. In this context, here we are

Partial purification and characterization of a novel soybean protease which is inhibited by Kunitz and Bowman-Birk trypsin inhibitors.

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A novel serine protease has been partially purified from dry seeds of the soybean (Glycine max) cultivar Keburi by cryoprecipitation at pH 6.4, fractional precipitation with ammonium sulfate, and a series of column chromatographic procedures on DEAE-Sepharose, SP-Sepharose, and Arginine-Sepharose

A proteomic study to identify soya allergens--the human response to transgenic versus non-transgenic soya samples.

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BACKGROUND In spite of being among the main foods responsible for allergic reactions worldwide, soybean (Glycine max)-derived products continue to be increasingly widespread in a variety of food products due to their well-documented health benefits. Soybean also continues to be one of the elected

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

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