Human non-secretory ribonucleases. I. Purification, peptide mapping and lectin blotting analysis of the kidney, liver and spleen enzymes |
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Authors: | Lawrence Cris W; Little Pamela A; Little Brian W; Miller Marsha J; Bazel Shamideh; Alhadeff Jack A |
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Institution: | 1Department of Chemistry and Center for Molecular Bioscience and Biotechnology, Iacocca Hall, 111 Research Drive, Lehigh University Bethlehem, PA 18015
2Neuropathology Laboratory, Lehigh Valley Hospital, 1200 South Cedar Crest Boulevard Allentown, PA 18105, USA |
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Abstract: | Human non-secretory neutral ribonucleases (RNases) from kidney,liver and spleen have been purified and characterized. SDSPAGEindicates that all three RNases are highly purified and haveapparent mol. wts of 1718 kDa. Kinetic analysis indicatesthat all three RNases have a broad pH optimum centred around6.5, and all three have similar substrate specificities withsignificant preference for RNA and poly(U) when compared topoly(C), poly (A) and poly(G). All of the above data, as wellas immunoblotting data using three polyclonal antibodies (anti-humanliver RNase, anti-human pancreatic RNase, anti-human eosino-phil-derivedneurotoxin), indicate that the three proteins are highly purifiedand are non-secretory RNases (IIN). Further characterizationby cyanogen bromide peptide mapping and extensive lectin blottingindicated no significant differences between the three humanRNases. All three RNases appear to have very similar, if notidentical, protein backbones and all three are glycoproteinswhich are recognized by lectins with specificity for GlcNAc,Fuc and, to a lesser extent, with specificity for Galß(14)GlcNAc.No significant tissuespecific differences were found among thethree human non-secretory RNases. lectin blotting non-secretory RNases peptide mapping |
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