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vicia/protease

הקישור נשמר בלוח
מאמריםניסויים קלינייםפטנטים
13 תוצאות

Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
A cDNA clone encoding a thiol-protease (TPE4A) was isolated from senescent ovaries of pea (Pisum sativum) by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequence of TPE4A has the conserved catalytic amino acids of papain. It is very similar to VSCYSPROA, a thiol-protease

[Purification and partial characterization of protease B from germinating vetch seeds].

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The sulfhydryl protease B was isolated from the cotyledons of 8-day old vetch seedlings and purified 1580-fold with a 38% recovery. The preparation obtained proved to be homogeneous by DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. The molecular weight of the enzyme as shown

Nodule-expressed Cyp15a cysteine protease genes map to syntenic genome regions in Pisum and Medicago spp.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
PsCyp15a is a gene that encodes a vacuolar cysteine protease expressed in wilt-induced shoots of Pisum sativum (pea) and in root nodules. To further the understanding of nodular PsCyp15a expression, a region 5' to the coding sequence of the gene was cloned. Varying lengths of 5' untranslated

Expression of sweet potato cysteine protease SPCP2 altered developmental characteristics and stress responses in transgenic Arabidopsis plants.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
In this report a full-length cDNA, SPCP2, which encoded a putative papain-like cysteine protease was isolated from senescent leaves of sweet potato (Ipomoea batatas). SPCP2 contained 1101 nucleotides (366 amino acids) in its open reading frame, and exhibited high amino acid sequence identities (ca.

Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Trypsin inhibitors from winter pea seeds (c.v. Frilene) have been purified by ammonium sulfate precipitation, gel filtration, and anion and cation exchange chromatography and shown to consist of six protease inhibitors (PSTI I, II, III, IVa, IVb, and V). Their molecular weights were determined by

[Participation of phenylalanine-p-nitroanilidase in the decomposition of reserve proteins of germinating vetch seeds].

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
L-phenylalanine-p-nitroanilidase (PPA-ase) from vetch cotyledons was purified 1600-fold with a 6.7% recovery. Data from gel electrophoresis suggest that the preparation obtained (specific activity 232 U/mg) contains only a small admixture of inactive protein. PPA-ase splits off more than 14% of

The structure of the lentil (Lens culinaris) lectin. Amino acid sequence determination and prediction of the secondary structure.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The subunit structure and complete amino acid sequence of the lectin extracted from Lens culinaris (LcL) seeds was determined. In previous studies, the primary structure of the alpha-chain (Mr = 5,710) was shown to be homologous to the alpha-chain of the lectin from Pisum sativum, the Vicia cracca
Oil palm (Elaeis guineensis Jacq.) somatic embryos differ from zygotic embryos in that they accumulate only small amounts of storage proteins. We compared the balance between deposition and degradation of storage proteins during zygotic or somatic embryogenesis and germinative growth in the two

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Narbonin is a 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons. Its amino acid composition and the pattern of its regulated accumulation in developing seeds led to the suggestion that narbonin could be a storage protein. Therefore, it was expected to be present

Cathepsin D inhibitor from Vicia sativa L.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Specific inhibitor of cathepsin D has been shown in the extract of Vicia sativa L. seeds. This inhibitor does not inhibit the activity of other aspartic proteases. Also it does not inhibit the activity of cysteine proteases and serine proteases.

Effects of cathepsin D inhibitor from Vicia sativa L. seed hulls on human skin fibroblasts and breast cancer cells (in vitro studies).

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Cathepsin D is a lysosomal protease which plays an important role in cancer invasion and metastasis. There are known inhibitors of that enzyme, such as pepstatin and potato inhibitor. In this study, we examined effects of the cathepsin D inhibitor from Vicia sativa L. seed hulls on cell cultures of

In Vitro Binding of Agrobacterium tumefaciens to Plant Cells from Suspension Culture.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
In vitro binding experiments were carried out using (32)P-labeled cells of the virulent Agrobacterium tumefaciens strain B6 and Datura innoxia cells from suspension culture. Binding kinetics showed that adherence of bacteria to Datura cells increased gradually during the first 60 minutes and
NodO is a secreted protein from Rhizobium leguminosarum bv. viciae with a role in signalling during legume nodulation. A Tn5-induced mutant was identified that was defective in NodO secretion. As predicted, the secretion defect decreased pea and vetch nodulation but only when the nodE gene was also
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