Purification of endopeptidase-24.11 (‘enkephalinase’) from pig brain by immunoadsorbent chromatography
نویسندگان
چکیده
منابع مشابه
Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography.
Membrane preparations from striatum of pig brain contain endopeptidase activity towards iodoinsulin B-chain. Only 50% of the hydrolysis of insulin B-chain is inhibitable by phosphoramidon, and DEAE-cellulose chromatography can resolve the phosphoramidon-sensitive and -insensitive activities. The former activity (now designated 'endopeptidase-24.11') is responsible for hydrolysis of [D-Ala2,Leu5...
متن کاملPurification of This Endopeptidase by Affinity Chromatography*
The endopeptidase, post-proline cleaving enzyme, has been purified 10,500-fold in an overall yield of 18% from lamb kidney. The enzyme possesses a specific activity of 45 ~mol/mg/min as tested with the substrate Z-Gly-Pro-Leu-Gly (K,,, = 6.0 x 10m5), has a molecular weight of 115,000, is comprised of two subunits with a molecular weight of 57,000, and exhibits maximal activity at pH 7.5 to 8.0....
متن کاملPurification and properties of a neurotensin-degrading endopeptidase from pig brain.
Neurotensin (NT) endopeptidase (EC 3.4.24.16) has been purified about 800-fold from pig brain by four sequential chromatographic steps depending on ion-exchange and hydrophobic interactions. Two types of preparation were studied: one from a Triton X-100-solubilized membrane fraction, and the other from the soluble fraction containing 90% or more of the total activity in the homogenate. NT endop...
متن کاملThe hydrolysis of endothelins by neutral endopeptidase 24.11 (enkephalinase).
Endothelins 1-3 are a family of 21-amino acid peptides whose structure consists of two rings formed by intra-chain disulfide bonds and a linear "COOH-terminal tail." These peptides were originally described on the basis of their potent vasoconstrictor activity. The hydrolytic inactivation of endothelin action has recently been implicated to be attributed, at least in part, to the enzyme neutral...
متن کاملPurification and properties of rabbit brain and liver 4-aminobutyrate aminotransferases isolated by monoclonal-antibody immunoadsorbent chromatography.
The use of a monoclonal-antibody immunoaffinity column for the rapid isolation of 4-aminobutyrate aminotransferases (EC 2.6.1.19) from rabbit brain and liver is described. Homogeneous enzyme protein is eluted from the immunoadsorbent with 100mM-citrate buffer, pH5, and remains stable at 4 degrees C for several days. One such column (bed volume 8 ml) has been used 40 times in a 9-month period to...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1983
ISSN: 0264-6021
DOI: 10.1042/bj2150519