Ribonuclease activity of sialic acid-binding lectin from Rana catesbeiana eggs. 1993

K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
Department of Biochemistry, Tohoku College of Pharmaceutical Sciences, Sendai, Japan.

Sialic acid-binding lectin (SBL) isolated from Rana catesbeiana eggs is a basic protein which agglutinates a large variety of tumour cells and has an amino acid sequence homologous to that of human angiogenin and pancreatic ribonuclease (RNase). Although SBL and angiogenin lack the Cys-65-Cys-72 disulphide bond of pancreatic RNase, the locations of the other three disulphide bonds are similar among the three molecules. SBL was found to exhibit RNase activity, as well as catalytic properties resembling those of bovine RNase A in some respects. For example, SBL hydrolyses poly(uridylic acid) and poly(cytidylic acid) as substrates, and prefers the former. RNase A and angiogenin are strongly inhibited by human placental RNase inhibitor, whereas the RNase activity and tumour cell agglutination activity of SBL are not affected by this inhibitor.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010063 Ovum A mature haploid female germ cell extruded from the OVARY at OVULATION. Egg,Egg, Unfertilized,Ova,Eggs, Unfertilized,Unfertilized Egg,Unfertilized Eggs
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D011892 Rana catesbeiana A species of the family Ranidae (true frogs). The only anuran properly referred to by the common name "bullfrog", it is the largest native anuran in North America. Bullfrog,Bullfrogs,Rana catesbeianas,catesbeiana, Rana
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003488 Cyanogen Bromide Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes. Bromide, Cyanogen
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
April 1987, Biochemistry,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
July 1996, International journal of oncology,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
July 1991, Biochemical and biophysical research communications,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
September 2001, Biological & pharmaceutical bulletin,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
December 2001, Biological & pharmaceutical bulletin,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
May 1997, Biological & pharmaceutical bulletin,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
November 1989, Journal of biochemistry,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
February 1995, Biological & pharmaceutical bulletin,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
December 2013, International journal of oncology,
K Nitta, and F Oyama, and R Oyama, and K Sekiguchi, and H Kawauchi, and Y Takayanagi, and S Hakomori, and K Titani
January 1983, Chemical & pharmaceutical bulletin,
Copied contents to your clipboard!