Reactivation of des(119â124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120
Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-Ser-Val-OH at the carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan: [Leu 120 ]-RNase 111â124, [Ile 120 ]-RNase 111...
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| Veröffentlicht in: | The Journal of biological chemistry 1972-08, Vol.247 (15), p.4768-4774 |
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| container_issue | 15 |
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| container_title | The Journal of biological chemistry |
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| creator | Lin, M C Gutte, B Caldi, D G Moore, S Merrifield, R B |
| description | Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-Ser-Val-OH at the
carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan:
[Leu 120 ]-RNase 111â124, [Ile 120 ]-RNase 111â124, [Trp 120 ]-RNase 111â124, [Ile 120 ]-RNase 113â124, [Leu 120 ]-RNase 115â124, [Ile 120 ]-RNase 115â124, [Trp 120 ]-RNase 115â124. The peptides were examined for their ability to regenerate enzymatic activity when mixed with RNase 1â118
which had been prepared by enzymatic degradation of RNase A. A study of the dissociation constants of the peptide-protein
complexes, of the Michaelis constants of the complexes with cyclic 2', 3'-cytidylic acid, and of the inhibition constants
with 2'-cytidylic acid led to the conclusion that Phe 120 plays an important role in binding the peptide and protein and in aligning the catalytic site of the complex, but that it
does not have a specific effect on binding of substrate. |
| doi_str_mv | 10.1016/S0021-9258(19)44977-6 |
| format | Article |
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carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan:
[Leu 120 ]-RNase 111â124, [Ile 120 ]-RNase 111â124, [Trp 120 ]-RNase 111â124, [Ile 120 ]-RNase 113â124, [Leu 120 ]-RNase 115â124, [Ile 120 ]-RNase 115â124, [Trp 120 ]-RNase 115â124. The peptides were examined for their ability to regenerate enzymatic activity when mixed with RNase 1â118
which had been prepared by enzymatic degradation of RNase A. A study of the dissociation constants of the peptide-protein
complexes, of the Michaelis constants of the complexes with cyclic 2', 3'-cytidylic acid, and of the inhibition constants
with 2'-cytidylic acid led to the conclusion that Phe 120 plays an important role in binding the peptide and protein and in aligning the catalytic site of the complex, but that it
does not have a specific effect on binding of substrate.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)44977-6</identifier><identifier>PMID: 5065952</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Carboxylic Acids ; Cattle ; Electrophoresis, Paper ; Enzyme Activation ; Histidine - analysis ; Isoleucine - chemical synthesis ; Isomerism ; Kinetics ; Leucine - chemical synthesis ; Peptides - chemical synthesis ; Peptides - isolation & purification ; Phenylalanine ; Protein Binding ; Resins, Plant - chemical synthesis ; Ribonucleases ; Spectrophotometry ; Tryptophan - chemical synthesis</subject><ispartof>The Journal of biological chemistry, 1972-08, Vol.247 (15), p.4768-4774</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-e928ba63448c9396f5e75117f8b0fd5684b51a32eb6638602a205e604eb57f583</citedby><cites>FETCH-LOGICAL-c379t-e928ba63448c9396f5e75117f8b0fd5684b51a32eb6638602a205e604eb57f583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5065952$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lin, M C</creatorcontrib><creatorcontrib>Gutte, B</creatorcontrib><creatorcontrib>Caldi, D G</creatorcontrib><creatorcontrib>Moore, S</creatorcontrib><creatorcontrib>Merrifield, R B</creatorcontrib><title>Reactivation of des(119â124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-Ser-Val-OH at the
carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan:
[Leu 120 ]-RNase 111â124, [Ile 120 ]-RNase 111â124, [Trp 120 ]-RNase 111â124, [Ile 120 ]-RNase 113â124, [Leu 120 ]-RNase 115â124, [Ile 120 ]-RNase 115â124, [Trp 120 ]-RNase 115â124. The peptides were examined for their ability to regenerate enzymatic activity when mixed with RNase 1â118
which had been prepared by enzymatic degradation of RNase A. A study of the dissociation constants of the peptide-protein
complexes, of the Michaelis constants of the complexes with cyclic 2', 3'-cytidylic acid, and of the inhibition constants
with 2'-cytidylic acid led to the conclusion that Phe 120 plays an important role in binding the peptide and protein and in aligning the catalytic site of the complex, but that it
does not have a specific effect on binding of substrate.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Carboxylic Acids</subject><subject>Cattle</subject><subject>Electrophoresis, Paper</subject><subject>Enzyme Activation</subject><subject>Histidine - analysis</subject><subject>Isoleucine - chemical synthesis</subject><subject>Isomerism</subject><subject>Kinetics</subject><subject>Leucine - chemical synthesis</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - isolation & purification</subject><subject>Phenylalanine</subject><subject>Protein Binding</subject><subject>Resins, Plant - chemical synthesis</subject><subject>Ribonucleases</subject><subject>Spectrophotometry</subject><subject>Tryptophan - chemical synthesis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM1qFEEQxxtR4pr4CIEGQZLDmK6e_sRTWNQEIhs2Ct6antkap2U-NtM9xr3lHXwDHyV5MWezS-pSh_9HFT9CjoF9AAbq7IYxDpnl0pyAPRXCap2pF2QGzORZLuHHSzJ7trwmb2L8xaYRFg7IgWRKWsln5H6Jvkzht0-h72hf0RXGEwD7-O_h_uEvcHFKl6Hou7Fs0Eek57TY0K_hTxoHpHch1fRm06UaUyjpfLG4yBIObeh8Q69xncLU9pFOMl32DW7rr2vsNo1vfBc6zICzI_Kq8k3Et_t9SL5__vRtfpFdLb5czs-vsjLXNmVouSm8yoUwpc2tqiRqCaArU7BqJZURhQSfcyyUyo1i3HMmUTGBhdSVNPkheb_rXQ_97YgxuTbEEpvpE-zH6AxIAVLzySh3xnLoYxywcushtH7YOGBuS949kXdbrA6seyLv1JQ73h8YixZXz6k96kl_t9Pr8LO-CwO6IvRlja3jQjuQTmhl8v_owops</recordid><startdate>19720810</startdate><enddate>19720810</enddate><creator>Lin, M C</creator><creator>Gutte, B</creator><creator>Caldi, D G</creator><creator>Moore, S</creator><creator>Merrifield, R B</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19720810</creationdate><title>Reactivation of des(119â124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120</title><author>Lin, M C ; Gutte, B ; Caldi, D G ; Moore, S ; Merrifield, R B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-e928ba63448c9396f5e75117f8b0fd5684b51a32eb6638602a205e604eb57f583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Carboxylic Acids</topic><topic>Cattle</topic><topic>Electrophoresis, Paper</topic><topic>Enzyme Activation</topic><topic>Histidine - analysis</topic><topic>Isoleucine - chemical synthesis</topic><topic>Isomerism</topic><topic>Kinetics</topic><topic>Leucine - chemical synthesis</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - isolation & purification</topic><topic>Phenylalanine</topic><topic>Protein Binding</topic><topic>Resins, Plant - chemical synthesis</topic><topic>Ribonucleases</topic><topic>Spectrophotometry</topic><topic>Tryptophan - chemical synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, M C</creatorcontrib><creatorcontrib>Gutte, B</creatorcontrib><creatorcontrib>Caldi, D G</creatorcontrib><creatorcontrib>Moore, S</creatorcontrib><creatorcontrib>Merrifield, R B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lin, M C</au><au>Gutte, B</au><au>Caldi, D G</au><au>Moore, S</au><au>Merrifield, R B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reactivation of des(119â124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1972-08-10</date><risdate>1972</risdate><volume>247</volume><issue>15</issue><spage>4768</spage><epage>4774</epage><pages>4768-4774</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-Ser-Val-OH at the
carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan:
[Leu 120 ]-RNase 111â124, [Ile 120 ]-RNase 111â124, [Trp 120 ]-RNase 111â124, [Ile 120 ]-RNase 113â124, [Leu 120 ]-RNase 115â124, [Ile 120 ]-RNase 115â124, [Trp 120 ]-RNase 115â124. The peptides were examined for their ability to regenerate enzymatic activity when mixed with RNase 1â118
which had been prepared by enzymatic degradation of RNase A. A study of the dissociation constants of the peptide-protein
complexes, of the Michaelis constants of the complexes with cyclic 2', 3'-cytidylic acid, and of the inhibition constants
with 2'-cytidylic acid led to the conclusion that Phe 120 plays an important role in binding the peptide and protein and in aligning the catalytic site of the complex, but that it
does not have a specific effect on binding of substrate.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>5065952</pmid><doi>10.1016/S0021-9258(19)44977-6</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1972-08, Vol.247 (15), p.4768-4774 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81541572 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Carboxylic Acids Cattle Electrophoresis, Paper Enzyme Activation Histidine - analysis Isoleucine - chemical synthesis Isomerism Kinetics Leucine - chemical synthesis Peptides - chemical synthesis Peptides - isolation & purification Phenylalanine Protein Binding Resins, Plant - chemical synthesis Ribonucleases Spectrophotometry Tryptophan - chemical synthesis |
| title | Reactivation of des(119â124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120 |
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