{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/82893"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/82893","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Studies of a low molecular weight Zn-containing protein population of lens tissue","abstract":"Maintenance of reduced protein sulfhydryl groups is an important function of lens metabolism. In an attempt to inter-relate how lens sulfhydryl metabolism, low molecular weight peptides and trace molecular weight Zn-containing protein population was studied. The concentration of rate lens Zn-containing protein population was studied. The concentration of rat lens Zn decreased 30% from day 10 to day 35 postpartum. After 6 weeks on a low-Zn diet, rats had 25% less lens Zn than control groups. Selenite-induced cataract did not affect lens Zn concentration. Of the total lens Zn, 25% was recovered in the ultrafiltration fraction of less than 20,000 molecular weight which contained 1% of the total soluble protein. Lens tissue has low molecular weight TCA-soluble components that can bind Hg. Isoelectric points of low molecular weight protein fractions were between pI 5.2-5.5. Polypeptide molecular weight was determined to be less than 5,000 daltons by gel filtration chromatography. Aggregation on SDS-polyacrylamide gel electrophoresis yielded apparent higher molecular weights of these proteins. Although the proteins isolated had metallothionein-like character in that they were of low molecular weight, contained Zn and had acidic pI values, the paucity of cysteine residues indicates that metallothionein is not a component of low molecular weight Zn-containing lens proteins.","abstract_html":"Maintenance of reduced protein sulfhydryl groups is an important function of lens metabolism. In an attempt to inter-relate how lens sulfhydryl metabolism, low molecular weight peptides and trace molecular weight Zn-containing protein population was studied. The concentration of rate lens Zn-containing protein population was studied. The concentration of rat lens Zn decreased 30% from day 10 to day 35 postpartum. After 6 weeks on a low-Zn diet, rats had 25% less lens Zn than control groups. Selenite-induced cataract did not affect lens Zn concentration. Of the total lens Zn, 25% was recovered in the ultrafiltration fraction of less than 20,000 molecular weight which contained 1% of the total soluble protein. Lens tissue has low molecular weight TCA-soluble components that can bind Hg. Isoelectric points of low molecular weight protein fractions were between pI 5.2-5.5. Polypeptide molecular weight was determined to be less than 5,000 daltons by gel filtration chromatography. Aggregation on SDS-polyacrylamide gel electrophoresis yielded apparent higher molecular weights of these proteins. Although the proteins isolated had metallothionein-like character in that they were of low molecular weight, contained Zn and had acidic pI values, the paucity of cysteine residues indicates that metallothionein is not a component of low molecular weight Zn-containing lens proteins.","abstract_has_math":false,"creators":["Schwab, Susan J."],"institution":"Virginia Polytechnic Institute and State University","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biochemistry and Nutrition","degree_department":"Biochemistry and Nutrition","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1982,"date_issued":"1982","date_published":"1982","updated_at":"2026-07-22T22:20:03Z","subjects":[],"languages":["en_US"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10919/82893","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Biochemistry and Nutrition"]},{"key":"dc:creator","label":"Author","values":["Schwab, Susan J."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2018-04-24T19:14:27Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2018-04-24T19:14:27Z"]},{"key":"dc:date.issued","label":"Date","values":["1982"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Polytechnic Institute and State University"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry and Nutrition"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/82893"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Maintenance of reduced protein sulfhydryl groups is an important function of lens metabolism. In an attempt to inter-relate how lens sulfhydryl metabolism, low molecular weight peptides and trace molecular weight Zn-containing protein population was studied. The concentration of rate lens Zn-containing protein population was studied. The concentration of rat lens Zn decreased 30% from day 10 to day 35 postpartum. After 6 weeks on a low-Zn diet, rats had 25% less lens Zn than control groups. Selenite-induced cataract did not affect lens Zn concentration. Of the total lens Zn, 25% was recovered in the ultrafiltration fraction of less than 20,000 molecular weight which contained 1% of the total soluble protein. Lens tissue has low molecular weight TCA-soluble components that can bind Hg. Isoelectric points of low molecular weight protein fractions were between pI 5.2-5.5. Polypeptide molecular weight was determined to be less than 5,000 daltons by gel filtration chromatography. Aggregation on SDS-polyacrylamide gel electrophoresis yielded apparent higher molecular weights of these proteins. Although the proteins isolated had metallothionein-like character in that they were of low molecular weight, contained Zn and had acidic pI values, the paucity of cysteine residues indicates that metallothionein is not a component of low molecular weight Zn-containing lens proteins."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Studies of a low molecular weight Zn-containing protein population of lens tissue"]}]}],"canonical_facts":{"dc:contributor.department":["Biochemistry and Nutrition"],"dc:creator":["Schwab, Susan J."],"dc:date.accessioned":["2018-04-24T19:14:27Z"],"dc:date.available":["2018-04-24T19:14:27Z"],"dc:date.issued":["1982"],"dc:description.abstract":["Maintenance of reduced protein sulfhydryl groups is an important function of lens metabolism. In an attempt to inter-relate how lens sulfhydryl metabolism, low molecular weight peptides and trace molecular weight Zn-containing protein population was studied. The concentration of rate lens Zn-containing protein population was studied. The concentration of rat lens Zn decreased 30% from day 10 to day 35 postpartum. After 6 weeks on a low-Zn diet, rats had 25% less lens Zn than control groups. Selenite-induced cataract did not affect lens Zn concentration. Of the total lens Zn, 25% was recovered in the ultrafiltration fraction of less than 20,000 molecular weight which contained 1% of the total soluble protein. Lens tissue has low molecular weight TCA-soluble components that can bind Hg. Isoelectric points of low molecular weight protein fractions were between pI 5.2-5.5. Polypeptide molecular weight was determined to be less than 5,000 daltons by gel filtration chromatography. Aggregation on SDS-polyacrylamide gel electrophoresis yielded apparent higher molecular weights of these proteins. Although the proteins isolated had metallothionein-like character in that they were of low molecular weight, contained Zn and had acidic pI values, the paucity of cysteine residues indicates that metallothionein is not a component of low molecular weight Zn-containing lens proteins."],"dc:description.degree":["Master of Science"],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["http://hdl.handle.net/10919/82893"],"dc:language.iso":["en_US"],"dc:publisher":["Virginia Polytechnic Institute and State University"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:title":["Studies of a low molecular weight Zn-containing protein population of lens tissue"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biochemistry and Nutrition"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:20:03Z"}