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Ribonuclease activity of sialic acid-binding lectin from Rana catesbeiana eggs |
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| Authors: | Nitta Kazuo; Oyama Fumitaka; Oyama Rieko; Sekiguchi Kiyotoshi; Kawauchi Hiroaki; Takayanagi Yoshio; Hakomori Sen-itiroh; Titani Koiti |
| Institution: | 1Department of Biochemistry, Cancer Research Institute, Tohoku College of Pharmaceutical Sciences Sendai 981 2Division of Biomedical Polymer Science, Institute of Comprehensive Medical Science, Fujita Health University Toyoake 470-11, Japan 3The Biomembrane Institute and University of Washington Seattle, WA 98119, USA |
| Abstract: | Sialic acid-binding lectin (SBL) isolated from Rana catesbeianaeggs is a basic protein which agglutinates a large variety oftumour cells and has an amino acid sequence homologous to thatof human angiogenin and pancreatic ribonuclease (RNase). AlthoughSBL and angiogenin lack the Cys-65-Cys-72 disulphide bond ofpancreatic RNase, the locations of the other three disulphidebonds are similar among the three molecules. SBL was found toexhibit RNase activity, as well as catalytic properties resemblingthose of bovine RNase A in some respects. For example, SBL hydrolysespoly(uridylic acid) and poly(cytidylic acid) as substrates,and prefers the former. RNase A and angiogenin are stronglyinhibited by human placental RNase inhibitor, whereas the RNaseactivity and tumour cell agglutination activity of SBL are notaffected by this inhibitor. |
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