Unique amino terminal structure of rat little gastrin
The heptadecapeptide form of rat gastrin was purified by a combination of DEAE cellulose, Sephadex G50, affinity, and high performance liquid chromatography. An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblockin...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1981-01, Vol.2 (4), p.453-458 |
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| container_title | Peptides (New York, N.Y. : 1980) |
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| creator | Reeve, Joseph R. Dimaline, Rodney Shively, John E. Hawke, David Chew, Peter Walsh, John H. |
| description | The heptadecapeptide form of rat gastrin was purified by a combination of DEAE cellulose, Sephadex G50, affinity, and high performance liquid chromatography. An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblocking reaction revealed the presence of one additional residue of arginine and proline compared with porcine gastrin. Microsequencing analysis of the unblocked peptide revealed that the sequence of the remaining hexadecapeptide was RPPMEEEEEAYGWMDF. The corresponding sequence of porcine gastrin is GPWMEEEEEAYGWMDF amide. The presence of carboxyl-terminal amide group in rat gastrin is strongly supported by complete immunoreactivity with antibodies specific for amidated C-terminal sequences of mammalian gastrins. The Arg and Pro substitutions in the amino terminal region can explain poor crossreactivity of rat gastrin with antibodies specific for the amino-terminal portion of porcine or human gastrin and its more basic chromatography pattern on ion exchange resins. |
| doi_str_mv | 10.1016/S0196-9781(81)80104-0 |
| format | Article |
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An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblocking reaction revealed the presence of one additional residue of arginine and proline compared with porcine gastrin. Microsequencing analysis of the unblocked peptide revealed that the sequence of the remaining hexadecapeptide was RPPMEEEEEAYGWMDF. The corresponding sequence of porcine gastrin is GPWMEEEEEAYGWMDF amide. The presence of carboxyl-terminal amide group in rat gastrin is strongly supported by complete immunoreactivity with antibodies specific for amidated C-terminal sequences of mammalian gastrins. 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An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblocking reaction revealed the presence of one additional residue of arginine and proline compared with porcine gastrin. Microsequencing analysis of the unblocked peptide revealed that the sequence of the remaining hexadecapeptide was RPPMEEEEEAYGWMDF. The corresponding sequence of porcine gastrin is GPWMEEEEEAYGWMDF amide. The presence of carboxyl-terminal amide group in rat gastrin is strongly supported by complete immunoreactivity with antibodies specific for amidated C-terminal sequences of mammalian gastrins. The Arg and Pro substitutions in the amino terminal region can explain poor crossreactivity of rat gastrin with antibodies specific for the amino-terminal portion of porcine or human gastrin and its more basic chromatography pattern on ion exchange resins.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Gastric Mucosa - analysis</subject><subject>Gastrins - isolation & purification</subject><subject>Human gastrin</subject><subject>Humans</subject><subject>PCA peptidase</subject><subject>Porcine gastrin</subject><subject>Pyloric Antrum - analysis</subject><subject>Rat Gastrin</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Swine</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotVZ_QmFPoofVmaS7mz2JFL-g4EF7DtnsrET2oyZZwX9vakuvQmBgnncyycPYHOEGAfPbN8AyT8tC4pXEawkIixSO2BRlIdIM8_KYTQ-RU3bm_ScALBalnLBJIXgpuZiybN3br5ES3dl-SAK5WHWb-OBGE0ZHydAkToektSG0lHzoSGx_zk4a3Xq62NcZWz8-vC-f09Xr08vyfpUaIcuQVjKrOGJjdC15xUkiCN4QCAmmaAzmEfKqyAygBC0ICiApYjsy0rEzY5e7ezduiK_0QXXWG2pb3dMwelUImQvkPAazXdC4wXtHjdo422n3oxDUVpf606W2LtT2bHUpiHPz_YKx6qg-TO39RH634xR_-W3JKW8s9YZq68gEVQ_2nw2_IaF5CQ</recordid><startdate>19810101</startdate><enddate>19810101</enddate><creator>Reeve, Joseph R.</creator><creator>Dimaline, Rodney</creator><creator>Shively, John E.</creator><creator>Hawke, David</creator><creator>Chew, Peter</creator><creator>Walsh, John H.</creator><general>Elsevier Inc</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>19810101</creationdate><title>Unique amino terminal structure of rat little gastrin</title><author>Reeve, Joseph R. ; Dimaline, Rodney ; Shively, John E. ; Hawke, David ; Chew, Peter ; Walsh, John H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-b85b211fcad82b2e81032fe0380c7fc162112b75c0180a3e070e83162fc1ea0a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Gastric Mucosa - analysis</topic><topic>Gastrins - isolation & purification</topic><topic>Human gastrin</topic><topic>Humans</topic><topic>PCA peptidase</topic><topic>Porcine gastrin</topic><topic>Pyloric Antrum - analysis</topic><topic>Rat Gastrin</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reeve, Joseph R.</creatorcontrib><creatorcontrib>Dimaline, Rodney</creatorcontrib><creatorcontrib>Shively, John E.</creatorcontrib><creatorcontrib>Hawke, David</creatorcontrib><creatorcontrib>Chew, Peter</creatorcontrib><creatorcontrib>Walsh, John H.</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>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reeve, Joseph R.</au><au>Dimaline, Rodney</au><au>Shively, John E.</au><au>Hawke, David</au><au>Chew, Peter</au><au>Walsh, John H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unique amino terminal structure of rat little gastrin</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>1981-01-01</date><risdate>1981</risdate><volume>2</volume><issue>4</issue><spage>453</spage><epage>458</epage><pages>453-458</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>The heptadecapeptide form of rat gastrin was purified by a combination of DEAE cellulose, Sephadex G50, affinity, and high performance liquid chromatography. An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblocking reaction revealed the presence of one additional residue of arginine and proline compared with porcine gastrin. Microsequencing analysis of the unblocked peptide revealed that the sequence of the remaining hexadecapeptide was RPPMEEEEEAYGWMDF. The corresponding sequence of porcine gastrin is GPWMEEEEEAYGWMDF amide. The presence of carboxyl-terminal amide group in rat gastrin is strongly supported by complete immunoreactivity with antibodies specific for amidated C-terminal sequences of mammalian gastrins. 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| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 1981-01, Vol.2 (4), p.453-458 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73863122 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Amino Acids - analysis Animals Chromatography, Affinity Chromatography, DEAE-Cellulose Chromatography, Gel Chromatography, High Pressure Liquid Gastric Mucosa - analysis Gastrins - isolation & purification Human gastrin Humans PCA peptidase Porcine gastrin Pyloric Antrum - analysis Rat Gastrin Rats Rats, Inbred Strains Swine |
| title | Unique amino terminal structure of rat little gastrin |
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