Human pancreatic proelastase 2. Sequence of the activation peptide
The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residu...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1980 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Protein Structure - Amsterdam : Elsevier, 623(1980), 1, Seite 208-212 |
| Übergeordnetes Werk: |
volume:623 ; year:1980 ; number:1 ; pages:208-212 |
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NLEJ186044178 |
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| 245 | 1 | 0 | |a Human pancreatic proelastase 2. Sequence of the activation peptide |
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| 520 | |a The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. | ||
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(DE-627)NLEJ186044178 (DE-599)GBVNLZ186044178 DE-627 ger DE-627 rakwb eng Human pancreatic proelastase 2. Sequence of the activation peptide 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Largman, C. oth Brodrick, J.W. oth Geokas, M.C. oth in BBA - Protein Structure Amsterdam : Elsevier 623(1980), 1, Seite 208-212 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:623 year:1980 number:1 pages:208-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90022-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 623 1980 1 208-212 |
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(DE-627)NLEJ186044178 (DE-599)GBVNLZ186044178 DE-627 ger DE-627 rakwb eng Human pancreatic proelastase 2. Sequence of the activation peptide 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Largman, C. oth Brodrick, J.W. oth Geokas, M.C. oth in BBA - Protein Structure Amsterdam : Elsevier 623(1980), 1, Seite 208-212 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:623 year:1980 number:1 pages:208-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90022-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 623 1980 1 208-212 |
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(DE-627)NLEJ186044178 (DE-599)GBVNLZ186044178 DE-627 ger DE-627 rakwb eng Human pancreatic proelastase 2. Sequence of the activation peptide 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Largman, C. oth Brodrick, J.W. oth Geokas, M.C. oth in BBA - Protein Structure Amsterdam : Elsevier 623(1980), 1, Seite 208-212 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:623 year:1980 number:1 pages:208-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90022-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 623 1980 1 208-212 |
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(DE-627)NLEJ186044178 (DE-599)GBVNLZ186044178 DE-627 ger DE-627 rakwb eng Human pancreatic proelastase 2. Sequence of the activation peptide 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Largman, C. oth Brodrick, J.W. oth Geokas, M.C. oth in BBA - Protein Structure Amsterdam : Elsevier 623(1980), 1, Seite 208-212 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:623 year:1980 number:1 pages:208-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90022-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 623 1980 1 208-212 |
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(DE-627)NLEJ186044178 (DE-599)GBVNLZ186044178 DE-627 ger DE-627 rakwb eng Human pancreatic proelastase 2. Sequence of the activation peptide 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Largman, C. oth Brodrick, J.W. oth Geokas, M.C. oth in BBA - Protein Structure Amsterdam : Elsevier 623(1980), 1, Seite 208-212 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:623 year:1980 number:1 pages:208-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90022-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 623 1980 1 208-212 |
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human pancreatic proelastase 2. sequence of the activation peptide |
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Human pancreatic proelastase 2. Sequence of the activation peptide |
| abstract |
The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. |
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The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. |
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The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1. |
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