Tryptic Digest of Papain

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Tryptic digest of papain. I. Isolation and sequence of some peptides from the oxidized protein.

Investigations are in progress in this laboratory to elucidate the amino acid sequence of the proteolytic enzyme, papain (2). Results have already been presented on the isolation and sequence of some peptides obtained after chymotryptic digestion of oxidized papain (3-5). In the present paper, we report the isolation, composition, and sequence of some peptides produced by tryptic digestion of o...

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Analysis of Glycopeptide Glycoforms in Monoclonal Antibody Tryptic Digest using a UPLC HILIC Column

Reversed-phase liquid chromatography (RP-LC) is a primary method chosen for protein characterization via peptide mapping. Peptide mapping applications require efficient columns to resolve complex peptide mixtures into unique peptides. Modified peptides, such as oxidized or deamidated ones, can also be separated from the unmodified peptides.1 UltraPerformance Liquid Chromatography® (UPLC®) techn...

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Chymotryptic digest of papain. III. Amino acid sequence of six peptides.

Dinitrophenylation-The amino-terminal residue was determined on. a sample of the peptide before desalting. Approximately 1 pmole of the peptide was submitted to dinitrophenylation for 6 hours with the reaction mixture maintained at pH 8.5 with the aid of a pH stat. The solution was evaporated to dryness and triturated with dry ethyl acetate. Estraction was continued until all the yellow color w...

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Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool.

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of th...

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LETTERS Intrinsic Amino Acid Size Parameters from a Series of 113 Lysine-Terminated Tryptic Digest Peptide Ions

Cross sections for mixtures of tryptic digest peptide ions formed by electrospray ionization have been measured by a new ion mobility/time-of-flight mass spectrometry technique. Analysis of a series of 113 peptides containing 5-10 residues and having a single lysine group located at the C-terminal end show that cross sections are largely dependent upon the amino acid composition of each peptide...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1965

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)97645-3