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Comparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1986
Unusual features of the T-cell receptor C domains are revealed by structural comparisons with other members of the immunoglobulin superfamilyD Beale, J CoadwellComparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1987
Tertiary structures for the extracellular domains of the epithelial polyimmunoglobulin receptor (secretory component) derived by primary structure comparisons with immunoglobulinsD Beale, J CoadwellComparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1983
A comparison of the fragmentation of different species of mammalian immunoglobulin M by trypsin in ureaD Beale, J HopleyThe International Journal of Biochemistry|January 1, 1989
Some observations on the replacement of the conserved amino acid residues of immunoglobulin domainsD Beale, J CoadwellBiochimica Et Biophysica Acta|April 30, 1987
The sites of tryptic cleavage in bovine secretory component: structural and functional implicationsD Beale, J CoadwellThe Biochemical Journal|March 15, 1985
Fragmentation and reduction of bovine secretory component. Preparation of a biologically active fragment and some evidence for a multiple-domain structureD Beale, J G HopleyThe Biochemical Journal|October 1, 1980
The action of pepsin on porcine immunoglobulin M and its effect on biological activityD Beale, J K FazakerleyBiochimica Et Biophysica Acta|September 29, 1981
A comparison of the actions of trypsin and pepsin on porcine immunoglobulin M and their effects on biological activityD Beale, J K FazakerleyInvestigative Ophthalmology & Visual Science|February 1, 1977
Radio telemetry of intraocular pressure in vitroR L Cooper, D BealeComparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1982
A comparison of the proteolytic fragmentation of immunoglobulin M from several different mammalian speciesD Beale, T Van DortPageof 10