Studies of a low molecular weight Zn-containing protein population of lens tissue

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.

Name thesis:degree_name

Master of Science

Level thesis:degree_level

masters

Discipline thesis:degree_discipline

Biochemistry and Nutrition

Department dc:contributor.department

Biochemistry and Nutrition

Grantor dc:publisher

Virginia Polytechnic Institute and State University

Year dc:date.issued

1982

Author dc:creator

• Schwab, Susan J.

Statement dc:rights

• In Copyright

Licence dc:rights.uri

• http://rightsstatements.org/vocab/InC/1.0/

Language dc:language.iso

en_US

Handle dc:identifier.uri

http://hdl.handle.net/10919/82893

OAI identifier oai:identifier

oai:vtechworks.lib.vt.edu:10919/82893