FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM

Different forms of DEAE-substituted ion exchange media (fibrous and microgranular cellulose and DEAE-Sephadex) produced essentially identical results in the chromatography of venom protein, although altering the experimental conditions resulted in markedly altered elution patterns. CM-cellulose, ove...

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1. Verfasser:	Reed,Donald E
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Schlagworte:	CHROMATOGRAPHIC ANALYSIS ELECTROPHORESIS ENZYMES INHIBITION IRON TRICARBONYL CYCLOBUTADIENE COMPLEXES MOLECULAR WEIGHT PEPTIDE HYDROLASES PROTEINS REPTILES TOXICITY Toxicology VENOMS
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description	Different forms of DEAE-substituted ion exchange media (fibrous and microgranular cellulose and DEAE-Sephadex) produced essentially identical results in the chromatography of venom protein, although altering the experimental conditions resulted in markedly altered elution patterns. CM-cellulose, over a wide pH range was ineffective in resolving protein components. Molecular sieve filtration of the lethal protein indicated that it behaved on Sephadex, Biogel and Sepharose as a very large molecule, with a molecular weight perhaps greater than 300,000. Preliminary examination of this same protein in the ultracentrifuge, however, did not indicate such a large protein. None of the methods described resulted in a protein which upon immunoelectrophoresis, produced a single precipitin band. (Author)
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CM-cellulose, over a wide pH range was ineffective in resolving protein components. Molecular sieve filtration of the lethal protein indicated that it behaved on Sephadex, Biogel and Sepharose as a very large molecule, with a molecular weight perhaps greater than 300,000. Preliminary examination of this same protein in the ultracentrifuge, however, did not indicate such a large protein. None of the methods described resulted in a protein which upon immunoelectrophoresis, produced a single precipitin band. (Author)</description><language>eng</language><subject>CHROMATOGRAPHIC ANALYSIS ; ELECTROPHORESIS ; ENZYMES ; INHIBITION ; IRON TRICARBONYL CYCLOBUTADIENE COMPLEXES ; MOLECULAR WEIGHT ; PEPTIDE HYDROLASES ; PROTEINS ; REPTILES ; TOXICITY ; Toxicology ; VENOMS</subject><creationdate>1967</creationdate><rights>APPROVED FOR PUBLIC RELEASE</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,776,881,27544,27545</link.rule.ids><linktorsrc>$$Uhttps://apps.dtic.mil/sti/citations/AD0659782$$EView_record_in_DTIC$$FView_record_in_$$GDTIC$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>Reed,Donald E</creatorcontrib><creatorcontrib>ARMY MEDICAL RESEARCH LAB FORT KNOX KY</creatorcontrib><title>FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM</title><description>Different forms of DEAE-substituted ion exchange media (fibrous and microgranular cellulose and DEAE-Sephadex) produced essentially identical results in the chromatography of venom protein, although altering the experimental conditions resulted in markedly altered elution patterns. CM-cellulose, over a wide pH range was ineffective in resolving protein components. Molecular sieve filtration of the lethal protein indicated that it behaved on Sephadex, Biogel and Sepharose as a very large molecule, with a molecular weight perhaps greater than 300,000. Preliminary examination of this same protein in the ultracentrifuge, however, did not indicate such a large protein. None of the methods described resulted in a protein which upon immunoelectrophoresis, produced a single precipitin band. (Author)</description><subject>CHROMATOGRAPHIC ANALYSIS</subject><subject>ELECTROPHORESIS</subject><subject>ENZYMES</subject><subject>INHIBITION</subject><subject>IRON TRICARBONYL CYCLOBUTADIENE COMPLEXES</subject><subject>MOLECULAR WEIGHT</subject><subject>PEPTIDE HYDROLASES</subject><subject>PROTEINS</subject><subject>REPTILES</subject><subject>TOXICITY</subject><subject>Toxicology</subject><subject>VENOMS</subject><fulltext>true</fulltext><rsrctype>report</rsrctype><creationdate>1967</creationdate><recordtype>report</recordtype><sourceid>1RU</sourceid><recordid>eNrjZAhxCw0K8XANUvB3CnYNCnMM8fT3C1bw91MACioEBPkHuAaFeLoCRdzAIj6uIR6OPiCJEFdPPwUgcgYyHX1CgxUcQ4L8IxTCXP38fXkYWNMSc4pTeaE0N4OMm2uIs4duSklmcnxxSWZeakm8o4uBmamluYWRMQFpAHpkLZE</recordid><startdate>19670915</startdate><enddate>19670915</enddate><creator>Reed,Donald E</creator><scope>1RU</scope><scope>BHM</scope></search><sort><creationdate>19670915</creationdate><title>FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM</title><author>Reed,Donald E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-dtic_stinet_AD06597823</frbrgroupid><rsrctype>reports</rsrctype><prefilter>reports</prefilter><language>eng</language><creationdate>1967</creationdate><topic>CHROMATOGRAPHIC ANALYSIS</topic><topic>ELECTROPHORESIS</topic><topic>ENZYMES</topic><topic>INHIBITION</topic><topic>IRON TRICARBONYL CYCLOBUTADIENE COMPLEXES</topic><topic>MOLECULAR WEIGHT</topic><topic>PEPTIDE HYDROLASES</topic><topic>PROTEINS</topic><topic>REPTILES</topic><topic>TOXICITY</topic><topic>Toxicology</topic><topic>VENOMS</topic><toplevel>online_resources</toplevel><creatorcontrib>Reed,Donald E</creatorcontrib><creatorcontrib>ARMY MEDICAL RESEARCH LAB FORT KNOX KY</creatorcontrib><collection>DTIC Technical Reports</collection><collection>DTIC STINET</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Reed,Donald E</au><aucorp>ARMY MEDICAL RESEARCH LAB FORT KNOX KY</aucorp><format>book</format><genre>unknown</genre><ristype>RPRT</ristype><btitle>FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM</btitle><date>1967-09-15</date><risdate>1967</risdate><abstract>Different forms of DEAE-substituted ion exchange media (fibrous and microgranular cellulose and DEAE-Sephadex) produced essentially identical results in the chromatography of venom protein, although altering the experimental conditions resulted in markedly altered elution patterns. CM-cellulose, over a wide pH range was ineffective in resolving protein components. Molecular sieve filtration of the lethal protein indicated that it behaved on Sephadex, Biogel and Sepharose as a very large molecule, with a molecular weight perhaps greater than 300,000. Preliminary examination of this same protein in the ultracentrifuge, however, did not indicate such a large protein. None of the methods described resulted in a protein which upon immunoelectrophoresis, produced a single precipitin band. (Author)</abstract><oa>free_for_read</oa></addata></record>
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subjects	CHROMATOGRAPHIC ANALYSIS ELECTROPHORESIS ENZYMES INHIBITION IRON TRICARBONYL CYCLOBUTADIENE COMPLEXES MOLECULAR WEIGHT PEPTIDE HYDROLASES PROTEINS REPTILES TOXICITY Toxicology VENOMS
title	FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM
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