Stabilization of proteins by guanidination
Earlier studies have indicated the marked resistance of two pronase endopeptidases to denaturation in high concentrations of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component has only a single residue of lysine and the other has n...
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creator | P Cupo W El-Deiry P L Whitney W M Awad, Jr |
description | Earlier studies have indicated the marked resistance of two pronase endopeptidases to denaturation in high concentrations
of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component
has only a single residue of lysine and the other has none. The consideration arose that lysine-containing peptide segments
may be less stable than those containing arginine because of the fluctuations of the side groups of the former residue. The
small epsilon amino groups may not be able to sustain solvation of the hydrophobic arm in an aqueous medium. Arginine residues
have shorter hydrophobic arms, larger hydrophilic groups, and higher pKa values and, thus may be less motile than lysine.
The hypothesis was tested by guanidination of seven globular proteins (bovine carbonic anhydrase, chymotrypsinogen, alpha-lactalbumin,
serum albumin, ribonuclease, hen egg lysozyme, and horse heart cytochrome c). Conversion of lysine residues to homoarginine
was between 90 and 99%. Tritium-hydrogen isotope exchange revealed that all proteins except lysozyme demonstrated reduced
out-exchange after guanidination. The results with lysozyme were not unexpected since only this protein has a high arginine
to lysine ratio. These findings suggest that high arginine to lysine ratios contribute to protein stability. |
doi_str_mv | 10.1016/S0021-9258(19)70382-2 |
format | Article |
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of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component
has only a single residue of lysine and the other has none. The consideration arose that lysine-containing peptide segments
may be less stable than those containing arginine because of the fluctuations of the side groups of the former residue. The
small epsilon amino groups may not be able to sustain solvation of the hydrophobic arm in an aqueous medium. Arginine residues
have shorter hydrophobic arms, larger hydrophilic groups, and higher pKa values and, thus may be less motile than lysine.
The hypothesis was tested by guanidination of seven globular proteins (bovine carbonic anhydrase, chymotrypsinogen, alpha-lactalbumin,
serum albumin, ribonuclease, hen egg lysozyme, and horse heart cytochrome c). Conversion of lysine residues to homoarginine
was between 90 and 99%. Tritium-hydrogen isotope exchange revealed that all proteins except lysozyme demonstrated reduced
out-exchange after guanidination. The results with lysozyme were not unexpected since only this protein has a high arginine
to lysine ratio. These findings suggest that high arginine to lysine ratios contribute to protein stability.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)70382-2</identifier><identifier>PMID: 6253487</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acids, Diamino - analysis ; Animals ; Carbonic Anhydrases ; Cattle ; Chymotrypsinogen ; Cytochrome c Group ; Drug Stability ; Guanidines ; Kinetics ; Lactalbumin ; Muramidase ; Proteins ; Ribonucleases ; Serum Albumin, Bovine</subject><ispartof>The Journal of biological chemistry, 1980-11, Vol.255 (22), p.10828-10833</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-631d178a109e46d29d7b8a386dfb4bf11e4367d5bc89c43b2f8abc108a4cb2153</citedby><cites>FETCH-LOGICAL-c380t-631d178a109e46d29d7b8a386dfb4bf11e4367d5bc89c43b2f8abc108a4cb2153</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/6253487$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>P Cupo</creatorcontrib><creatorcontrib>W El-Deiry</creatorcontrib><creatorcontrib>P L Whitney</creatorcontrib><creatorcontrib>W M Awad, Jr</creatorcontrib><title>Stabilization of proteins by guanidination</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Earlier studies have indicated the marked resistance of two pronase endopeptidases to denaturation in high concentrations
of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component
has only a single residue of lysine and the other has none. The consideration arose that lysine-containing peptide segments
may be less stable than those containing arginine because of the fluctuations of the side groups of the former residue. The
small epsilon amino groups may not be able to sustain solvation of the hydrophobic arm in an aqueous medium. Arginine residues
have shorter hydrophobic arms, larger hydrophilic groups, and higher pKa values and, thus may be less motile than lysine.
The hypothesis was tested by guanidination of seven globular proteins (bovine carbonic anhydrase, chymotrypsinogen, alpha-lactalbumin,
serum albumin, ribonuclease, hen egg lysozyme, and horse heart cytochrome c). Conversion of lysine residues to homoarginine
was between 90 and 99%. Tritium-hydrogen isotope exchange revealed that all proteins except lysozyme demonstrated reduced
out-exchange after guanidination. The results with lysozyme were not unexpected since only this protein has a high arginine
to lysine ratio. These findings suggest that high arginine to lysine ratios contribute to protein stability.</description><subject>Amino Acids, Diamino - analysis</subject><subject>Animals</subject><subject>Carbonic Anhydrases</subject><subject>Cattle</subject><subject>Chymotrypsinogen</subject><subject>Cytochrome c Group</subject><subject>Drug Stability</subject><subject>Guanidines</subject><subject>Kinetics</subject><subject>Lactalbumin</subject><subject>Muramidase</subject><subject>Proteins</subject><subject>Ribonucleases</subject><subject>Serum Albumin, Bovine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLAzEUhYMotVZ_QmEWIiqM5iaTmWQpxRcUXFTBXchr2sg8dDKD1F9v-qB3cxfnnHsPH0JTwHeAIb9fYEwgFYTxaxA3BaacpOQIjQFzmlIGn8dofLCcorMQvnCcTMAIjXLCaMaLMbpd9Er7yv-p3rdN0pbJd9f2zjch0etkOajGW99sxXN0UqoquIv9nqCPp8f32Us6f3t-nT3MU0M57tOcgoWCK8DCZbklwhaaK8pzW-pMlwAuo3lhmTZcmIxqUnKlTWytMqMJMDpBV7u7scnP4EIvax-MqyrVuHYIsmCUcCaKaGQ7o-naEDpXyu_O16pbS8Byw0huGckNAAlCbhlJEnPT_YNB184eUnsoUb_c6Su_XP36zkntW7NytSSMSULibU44_QdVB20p</recordid><startdate>19801125</startdate><enddate>19801125</enddate><creator>P Cupo</creator><creator>W El-Deiry</creator><creator>P L Whitney</creator><creator>W M Awad, Jr</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>19801125</creationdate><title>Stabilization of proteins by guanidination</title><author>P Cupo ; W El-Deiry ; P L Whitney ; W M Awad, Jr</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-631d178a109e46d29d7b8a386dfb4bf11e4367d5bc89c43b2f8abc108a4cb2153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Amino Acids, Diamino - analysis</topic><topic>Animals</topic><topic>Carbonic Anhydrases</topic><topic>Cattle</topic><topic>Chymotrypsinogen</topic><topic>Cytochrome c Group</topic><topic>Drug Stability</topic><topic>Guanidines</topic><topic>Kinetics</topic><topic>Lactalbumin</topic><topic>Muramidase</topic><topic>Proteins</topic><topic>Ribonucleases</topic><topic>Serum Albumin, Bovine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>P Cupo</creatorcontrib><creatorcontrib>W El-Deiry</creatorcontrib><creatorcontrib>P L Whitney</creatorcontrib><creatorcontrib>W M Awad, Jr</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>P Cupo</au><au>W El-Deiry</au><au>P L Whitney</au><au>W M Awad, Jr</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization of proteins by guanidination</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1980-11-25</date><risdate>1980</risdate><volume>255</volume><issue>22</issue><spage>10828</spage><epage>10833</epage><pages>10828-10833</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Earlier studies have indicated the marked resistance of two pronase endopeptidases to denaturation in high concentrations
of urea or guanidine hydrochloride (Siegel, S., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 3233--3240). One component
has only a single residue of lysine and the other has none. The consideration arose that lysine-containing peptide segments
may be less stable than those containing arginine because of the fluctuations of the side groups of the former residue. The
small epsilon amino groups may not be able to sustain solvation of the hydrophobic arm in an aqueous medium. Arginine residues
have shorter hydrophobic arms, larger hydrophilic groups, and higher pKa values and, thus may be less motile than lysine.
The hypothesis was tested by guanidination of seven globular proteins (bovine carbonic anhydrase, chymotrypsinogen, alpha-lactalbumin,
serum albumin, ribonuclease, hen egg lysozyme, and horse heart cytochrome c). Conversion of lysine residues to homoarginine
was between 90 and 99%. Tritium-hydrogen isotope exchange revealed that all proteins except lysozyme demonstrated reduced
out-exchange after guanidination. The results with lysozyme were not unexpected since only this protein has a high arginine
to lysine ratio. These findings suggest that high arginine to lysine ratios contribute to protein stability.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6253487</pmid><doi>10.1016/S0021-9258(19)70382-2</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Amino Acids, Diamino - analysis Animals Carbonic Anhydrases Cattle Chymotrypsinogen Cytochrome c Group Drug Stability Guanidines Kinetics Lactalbumin Muramidase Proteins Ribonucleases Serum Albumin, Bovine |
title | Stabilization of proteins by guanidination |
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