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دانلود رایگان Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seedsPurification and partial characterization of aminopeptidase from barley : Hordeum vulgare L. seeds
اين مقاله مربوط به گياه جو بوده كه در سال 2013 در سايت ساينس دايركت نمايه شده است اين مقاله 6 صفحه بوده و فرمت آن pdf است.
Aminopeptidases
Barley seeds
Purification
Characterization
مقاله
پاورپوینت
فایل فلش
کارآموزی
گزارش تخصصی
اقدام پژوهی
درس پژوهی
جزوه
خلاصه
The influence of α-aminophosphonic acids on the …
Abstract. Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metallo-aminopeptidase have been determined to evaluate structural requirements of this enzyme.The enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine …
Characteristics of an Aminopeptidase from …
Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds. Plant Physiology and Biochemistry 2013, 65, 75-80. ... Identification of a plant aminopeptidase with preference for aromatic amino acid residues as a novel member of the prolyl oligopeptidase family of serine proteases.
Purification and Partial Characterization of a …
It was previously shown that ungerminated barley contains inhibitors that suppress the activities of green malt cysteine proteinases. This paper reports the purification and partial characterization of a second barley cysteine endoproteinase inhibitor, a protein called lipid transfer protein 2 (LTP2). The chromatographically purified inhibitor had a molecular mass of 7112.
Purification and partial characterization of ...
Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds Author links open overlay panel Bartosz Oszywa Maciej Makowski 1 …
Purification and partial characterization of ...
01/04/2013 · Aminopeptidases (EC 3.4.11) are proteolytic enzymes, which hydrolyze one amino acid from N-terminus of peptidic substrates. Inhibitors of plant aminop…
[PDF] Purification and partial characterization of …
A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties. It has a sedimentation constant of 12.7S and a ...
Purification and Partial Characterization of Barley ...
01/05/1975 · A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties.
(PDF) Purification and partial characterization of ...
Purification and partial characterization of aminopeptidase from barley ... Isolation and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds has been described.
Literature for peptidase M17.002: leucyl …
Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds. Plant Physiol Biochem (2013) 65 , 75-80. PubMed Europe PubMed DOI P
[PDF] Purification and partial characterization of …
A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties. It has a sedimentation constant of 12.7S and a ...
Purification and Partial Characterization of a …
It was previously shown that ungerminated barley contains inhibitors that suppress the activities of green malt cysteine proteinases. This paper reports the purification and partial characterization of a second barley cysteine endoproteinase inhibitor, a protein called lipid transfer protein 2 (LTP2). The chromatographically purified inhibitor had a molecular mass of 7112.
Purification and partial characterization of a …
Purification and partial characterization of a dipeptidase from barley A peptidase hydrolyzing the dipeptide Ala-Gly optimally at pH 8 to 9 was purified about 3500-fold …
Purification and characterization of three soluble ...
Unger C, Hofsteenge J, Sturm A. Purification and characterization of a soluble beta-fructofuranosidase from Daucus carota. Eur J Biochem. 1992 Mar 1; 204 (2):915–921. Wagner W, Wiemken A, Matile P. Regulation of Fructan Metabolism in Leaves of Barley (Hordeum vulgare L. cv Gerbel). Plant Physiol. 1986 Jun; 81 (2):444–447.
The influence of α-aminophosphonic acids on the …
Abstract. Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metallo-aminopeptidase have been determined to evaluate structural requirements of this enzyme.The enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine …
Purification and Partial Characterization of Barley ...
01/05/1975 · A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties.
(PDF) Purification and partial characterization of ...
Purification and partial characterization of aminopeptidase from barley ... Isolation and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds has been described.
Purification and Partial Characterization of …
Purification and Partial Characterization of Barley Leucine Aminopeptidase . By Tuomas Sopanen and Juhani Mikola. Abstract. A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.).
[PDF] Purification and partial characterization of …
A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties. It has a sedimentation constant of 12.7S and a ...
Purification and partial characterization of ...
01/04/2013 · Aminopeptidases (EC 3.4.11) are proteolytic enzymes, which hydrolyze one amino acid from N-terminus of peptidic substrates. Inhibitors of plant aminop…
The influence of α-aminophosphonic acids on the …
Abstract. Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metallo-aminopeptidase have been determined to evaluate structural requirements of this enzyme.The enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine …
Preparation and characterization of antimicrobial ...
01/09/2015 · Preparation and characterization of antimicrobial cationized peptides from barley (Hordeum vulgare L.) proteins. Author links open overlay ... Hordeum vulgare L. 1. ... more stable charge density in neutral pH range as well as the simple modification and purification steps have implications to the utilization of these cationized ...
Purification and partial characterization of ...
Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds Author links open overlay panel Bartosz Oszywa Maciej Makowski 1 …
Purification and Partial Characterization of an ...
Hordeum vulgare L. xylanase inhibitor (HVXI), an endoxylanase inhibitor with a protein structure, was purified to homogeneity from barley (Hordeum vulgare L.). HVXI is a nonglycosylated monomeric protein, with a molecular weight of ≈40,000 and a pI ≥ 9.3. Although it inhibits different endoxylanases to a varying degree, the activities of an α‐L‐arabinofuranosidase and a β‐ d ...
[PDF] Purification and partial characterization of …
A peptidase acting on Leu-Gly-Gly and Leu-Tyr at pH 8 to 10 was purified about 670-fold from germinated grains of barley (Hordeum vulgare L.). Gel electrophoretic analyses indicated a purity of about 90%. The purified enzyme is remarkably similar to mammalian leucine aminopeptidases (EC 3.4.1.1) both in chemical and in enzymatic properties. It has a sedimentation constant of 12.7S and a ...
Purification and Characterization of Barley …
Barley ( Hordeum vulgare L.) storage proteins, which have a high content of proline (Pro) and glutamine, are cleaved by cysteine endoproteases to yield peptides with a Pro next to the N-terminal and/or C-terminal amino acid residues. A peptidase cleaving after Xaa-Pro- at the N terminus of peptides was purified from green barley malt. It was identified as a serine-type dipeptidyl peptidase ...