canavalia oxyphylla/protease

Sábháiltear an nasc chuig an gearrthaisce

AiltTrialacha cliniciúlaPaitinní

Roghnaigh cineál sórtála

Leathanach 1 ó 25 torthaí

Interaction of proteases with legume seed inhibitors. Molecular features.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

After having found that raw black beans (Phaseolus vulgaris) were toxic, while the cooked ones constitute the basic diet of the underdeveloped peoples of the world, in the sixties, our research directed by Dr. Jaffé, concentrated mainly around the detection and identification of the heat labile

Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts

Urease and serine protease inhibitory alkaloids from Isatis tinctoria.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

Phytochemical investigations on the alkaloidal fraction of the whole plant of the Isatis tinctoria led to the isolation of the alkaloids 1-6., 3'-Hydroxyepiglucoisatisin (3), Epiglucoisatisin (2) were found to be potent urease inhibitors in a concentration-dependent manner with IC(50) values 25.63

Corrigendum to "Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology".

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

[This corrects the article DOI: 10.1155/2016/3427098.].

Natural plant enzyme inhibitors: isolation and properties of a trypsin inhibitor from jack bean (Canavalia ensiformis).

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

A protease inhibitor which is equally active on bovine and porcine trypsins was isolated in a homogenous form from jack bean (Canavalia ensiformis). The preparation with a molecular weight of 18 kDa was found to be a glycoprotein with a high half cysteine content. Isoleucine and tyrosine were found

Purification and characterization of a basic amino acid-specific peptidase from seeds of jack bean (Canavalia ensiformis).

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

A peptidase was purified from seeds of Canavalia ensiformis by extraction with water, ammonium sulfate precipitation, and successive chromatographies on DEAE-Toyopearl 650M, butyl-Toyopearl 650M, and G-3000 SW columns. The enzyme has an apparent molecular weight of 41,000. Activity is maximal at pH

[Effect of extrusion on the activity of anti-nutritional factors and in vitro digestibility of protein and starch in flours of Canavalia ensiformis].

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

The effect of the extrusion (155 degrees C, 20% moisture, screw speed 75 rpm, feed speed 205 g min-1) on antinutritional factors of Canavalia ensiformis was studied. In vitro protein and starch digestibilities were assessed. The extrusion not affect protein content (23%) in the flours, but

Amino acid sequences of double-headed proteinase inhibitors from the seeds of Canavalia lineata.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

The amino acids of two Bowman-Birk type proteinase inhibitors (CLTI-I and -II) from the seeds of Canavalia lineata were sequenced by a manual Edman degradation using the DABITC/PITC double coupling method after enzymatic digestions with Achromobacter lyticus lysyl endopeptidase, Staphylococcus

Purification and characterization of two Kunitz family subtilisin inhibitors from seeds of Canavalia lineata.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

Two subtilisin inhibitors (CLSI-II and -III) were purified from seeds of Canavalia lineata by extraction with water, ammonium sulfate precipitation, and chromatographies on DEAE-Toyopearl and hydroxyapatite. The two inhibitors have the same molecular weight of about 22,000, and quite similar amino

Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

The degradation of peroxisomal and nonperoxisomal proteins by endoproteases of purified peroxisomes from senescent pea (Pisum sativum L.) leaves has been investigated. In our experimental conditions, most peroxisomal proteins were endoproteolytically degraded. This cleavage was prevented, to some

Comparison of the amino acid sequences of the lectins from seeds of Dioclea lehmanni and Canavalia maritima.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

The amino acid sequences of the major lectins from the seeds of Dioclea lehmanni and Canavalia maritima were determined by DABITC/PITC microsequence analysis of peptides derived from the proteins by enzymatic digestions with trypsin, chymotrypsin and the protease from S. aureus V8. These sequences

Property and amino acid sequence of a subtilisin inhibitor from seeds of beach canavalia (Canavalia lineata).

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

A subtilisin inhibitor was purified from the seeds of Canavalia lineata by ammonium sulfate precipitation, ultrafiltration on a YM-30 membrane, column chromatography on DEAE-Toyopearl and SP-Toyopearl, followed by reverse-phase HPLC. The inhibitor (CLSI-I) is a low molecular weight protein (M(r)

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

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

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

Threonine is present instead of cysteine at the active site of urease from Staphylococcus xylosus.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

DNA sequence analysis of the structural urease genes from Staphylococcus xylosus revealed that three enzyme subunits are encoded in the order of 11,000, 15,400 and 61,000 (mol. mass), which correspond to the single polypeptide chain of jack bean urease (90,800). Comparing the deduced amino acid

Delineation of the lectin site of the molecular chaperone calreticulin.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

Calreticulin (CRT) is a soluble molecular chaperone of the endoplasmic reticulum that functions to promote protein folding as well as to retain misfolded proteins. Similar to its membrane-bound paralog calnexin (CNX), CRT is a lectin that preferentially interacts with glycoproteins bearing

Roimhe seo
1
2
Ar Aghaidh

Bí ar ár
leathanach facebook

Herbal & Natural Medicine

An bunachar luibheanna míochaine is iomláine le tacaíocht ón eolaíocht

Oibreacha i 55 teanga
Leigheasanna luibhe le tacaíocht ón eolaíocht
Aitheantas luibheanna de réir íomhá
Léarscáil GPS idirghníomhach - clibeáil luibheanna ar an láthair (ag teacht go luath)
Léigh foilseacháin eolaíochta a bhaineann le do chuardach
Cuardaigh luibheanna míochaine de réir a n-éifeachtaí
Eagraigh do chuid spéiseanna agus fanacht suas chun dáta leis an taighde nuachta, trialacha cliniciúla agus paitinní

Clóscríobh symptom nó galar agus léigh faoi luibheanna a d’fhéadfadh cabhrú, luibh a chlóscríobh agus galair agus comharthaí a úsáidtear ina choinne a fheiceáil.
* Tá an fhaisnéis uile bunaithe ar thaighde eolaíoch foilsithe