Purification and Characterization of a Novel Aminopeptidase, Plastidial Alanine-Aminopeptidase, from the Cotyledons of Etiolated Sugar Beet Seedlings
نویسندگان
چکیده
منابع مشابه
Purification and properties of an alanine aminopeptidase from camel liver
Article history: Received on: 03/10/2016 Accepted on: 20/01/2017 Available online: 30/05/2017 Alanine aminopeptidase is purified from camel liver to homogeneity and designated CLAAP. The purification procedure involved anion exchange chromatography on DEAE-cellulose column and gel filtration chromatography on Sephacryl S-300 column. The specific activity of CLAAP is increased to 9.9 folds over ...
متن کاملwuthering heights and the concept of marality/a sociological study of the novel
to discuss my point, i have collected quite a number of articles, anthologies, and books about "wuthering heights" applying various ideas and theories to this fantastic story. hence, i have come to believe that gadamer and jauss are rightful when they claim that "the individaul human mind is the center and origin of all meaning," 3 that reading literature is a reader-oriented activity, that it ...
15 صفحه اولPurification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii.
A prolyl aminopeptidase (PAP) (EC 3.4.11.5) was isolated from the cell extract of Debaryomyces hansenii CECT12487. The enzyme was purified by selective fractionation with protamine and ammonium sulfate, followed by two chromatography steps, which included gel filtration and anion-exchange chromatography. The PAP was purified 248-fold, with a recovery yield of 1.4%. The enzyme was active in a br...
متن کاملPurification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae.
Methionine aminopeptidase (MAP), which catalyzes the removal of NH2-terminal methionine from proteins, was isolated from Saccharomyces cerevisiae. The enzyme was purified 472-fold to apparent homogeneity. The Mr of the native enzyme was estimated to be 36,000 +/- 5,000 by gel filtration chromatography, and the Mr of the denatured protein was estimated to be 34,000 +/- 2,000 by sodium dodecyl su...
متن کاملImmunoaffinity purification and characterization of leucine aminopeptidase from human liver.
Leucine aminopeptidase was purified from human liver cytosol to homogeneity, 1538-fold, with a yield of 84.4% by immunoaffinity chromatography. Increases in the activity and the stability of the enzyme were simultaneously observed during the purification procedure, suggesting the presence of some endogenous inhibitor in cytosol. The specific activity and Km value of the enzyme for L-leucine ami...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 1995
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.109.1.87