Amino acid sequence of porcine spleen cathepsin D.
نویسندگان
چکیده
منابع مشابه
Amino acid sequence of porcine spleen cathepsin D.
The amino acid sequence of porcine spleen cathepsin D heavy chain has been determined and, hence, the complete structure of this enzyme is now known. The sequence of heavy chain was constructed by aligning the structures of peptides generated by cyanogen bromide, trypsin, and endo-proteinase Lys C cleavages. The structure of the light chain has been published previously. The cathepsin D molecul...
متن کاملOligosaccharide units of lysosomal cathepsin D from porcine spleen. Amino acid sequence and carbohydrate structure of the glycopeptides.
The amino acid sequences near the glycosylation sites and the oligosaccharide structures have been determined for the lysosomal protease cathepsin D from porcine spleen. Cathepsin D light and heavy chains were separately digested with proteases and the glycopeptides were purified. A single sequence was constructed from the amino acid sequence of the light chain glycopeptides which is: Tyr-Asn-S...
متن کاملPurification and properties of cathepsin D from porcine spleen.
Cathepsin D was purified from porcine spleen to near homogeneity as determined by gel electrophoresis. The isolation scheme involved an acid precipitation of tissue extract, DEAE-cellulose and Sephadex G-200 chromatography, and isoelectric focusing. The end product represented about a 1000-fold purification and about a 10% recovery. The purified enzyme was the major isoenzyme, which represented...
متن کاملAmino acid sequence of porcine neurophysin-I.
Tryptic and chymotryptic peptide fragments obtained from performic acid-oxidized porcine neurophysin-I were isolated and purified by gel filtration, ion exchange chromatography, paper electrophoresis, and paper chromatography. The larger tryptic peptides were further hydrolyzed by papain, chymotrypsin, pepsin, or HCl to yield shorter fragments amenable to Edman degradation. The sum of the compo...
متن کاملAmino-acid sequence of porcine pepsin.
As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the s...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1984
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.81.12.3703