摘要:

Bovine retinal S-antigen was cleaved by three chemical cleavage procedures includingo-iodosobenzoic acid (IBA), mild acid and cyanogen bromide. The resultant peptides were used to study antibody-defined epitopes. Treatment with IBA, which cleaves primarily at tryptophanyl peptide bonds, produced at least 4 major fragments and several minor fragments. The peptides have been identified by their migration on SDS-PAGE and tested for their immunoreactivity to several affinity-purified anti-CNBr-peptide antibodies and to affinity-purified anti-IBA peptide antibodies. The presence of a single tryptophan residue 194 residues from the amino-terminus should result in 2 fragments of approximately 23,000 and 26,000 molecular weight based on the known size of intact S-antigen. The additional fragmentation is due to the presence of acid labile bonds and cleavage at IBA-sensitive tyrosyl residues associated with a side reaction. Western immunoblots using affinity-purified antibodies against the various IBA and CNBr peptides have allowed location of these peptides within the intact molecule. Specifically, IBA23K and IBA21K are overlapping fragments on the carboxy end, mutually exclusive of all other peptides. IBA15K and IBA5.6K overlap, and IBA18K and IBA10K overlap within IBA26K which comprises the N-terminal half of S-Ag. Additionally, IBA10K contains an antibody epitope destroyed by CNBr cleavage of the methionyl residue between CB53 and CB56. Further characterization of these IBA peptides will expedite the location of possible additional uveitogenic epitopes in the amino-terminal half of S-Ag as well as epitopes lost by other peptide generating techniques.

ISSN:0271-3683    

DOI:10.3109/02713688808995748

出版商:Taylor&Francis    

年代:1988

数据来源: Taylor

摘要:

The indices employed commonly for the diagnosis of glaucoma (tonometry, ophthalmoscopy and perimetry) do not always identify which patients with ocular hypertension (OHT) will develop primary open-angle glaucoma (POAG) before irreversible visual field loss is manifest (1). The human pattern reversal electroretinogram (PRERG) is a bioelectric response reflecting neural activity of the proximal retina. PRERG amplitude reductions have been observed in POAG and other diseases affecting the optic nerve and retinal ganglion cells. This study was designed to determine whether OHT patients exhibit PRERG amplitude reductions and whether PRERG results are correlated with routinely evaluated clinical parameters. Steady-state PRERG (16 rps) were elicited by high contrast (76%), phase alternating checkerboard patterns (15–20 min checks) from one eye of 130 patients with ocular hypertension and 47 age matched visual normals (AMVNs). A significant (p<0.05) reduction in PRERG amplitude was noted for the OHT patients and 11.5% of those patients exhibited PRERG amplitudes more than 2.0 standard deviations below the AMVN mean. PRERG amplitude was found to be positively correlated with diastolic blood pressure (DBP) and negatively correlated with age, but no correlation between PRERG amplitude and either IOP, C/D ratio, or systolic blood pressure was evident. The lack of correlation between PRERG amplitude and the commonly used clinical indices may suggest a complementary role for this neurophysiologic test in determining which OHT patients will develop glaucoma.

ISSN:0271-3683    

DOI:10.3109/02713688808995749

出版商:Taylor&Francis    

年代:1988

数据来源: Taylor

摘要:

A major protein with a molecular weight of 17,000, designated as MP17, has been identified in mammalian eye lens plasma membranes. Hydrophobic photolabeling experiments revealed that MP17 is a genuine intrinsic membrane protein. By using monoclonal antibodies we demonstrated that MP17 is not detectable in liver, heart, muscle, spleen and kidney, and thus can be considered, like MP26, as a lens-specific membrane protein. Furthermore, we showed that MP17 is a substrate for cAMP-dependent protein kinase and that it is a calmodulin-binding protein.

ISSN:0271-3683    

DOI:10.3109/02713688808995750

出版商:Taylor&Francis    

年代:1988

数据来源: Taylor