Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana
Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1991-05, Vol.109 (5), p.786-790 |
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| creator | Okabe, Yukie Katayama, Naoko Iwama, Masanori Watanabe, Hideaki Ohgi, Kazuko Irie, Masachika Nitta, Kazuo Kawauchi, Hiroaki Takayanagi, Yoshio Oyama, Fumitaka Yasuko Abe, Koichl Titani Okazaki, Taro Inokuchi, Norio Koyama, Takashi |
| description | Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The base specificities of the B1 and B2 sites of these proteins are U>C and G>U>A, C, respectively. The three frog proteins are more resistant than RNase A to heat treatment, guanidine-HCl and pH-induced denaturation; i.e.,they retain their native conformation up to at least 70°C at pH 7.5. Differences in stability and base specificity among RNase A and the three frog proteins are discussed in relation to the primary structures. Although the two lectins agglutinate tumor cells (e.g., Ehrlich, S-180 and AH109A ascites carcinoma cells), the liver RNase has no such activity. Agglutination of AH109A cells by the two lectins is inhibited by nucleotides. Our results indicate that the agglutination sites are not identical with, but are related to, the active sites of the three frog proteins. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a123457 |
| format | Article |
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The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The base specificities of the B1 and B2 sites of these proteins are U>C and G>U>A, C, respectively. The three frog proteins are more resistant than RNase A to heat treatment, guanidine-HCl and pH-induced denaturation; i.e.,they retain their native conformation up to at least 70°C at pH 7.5. Differences in stability and base specificity among RNase A and the three frog proteins are discussed in relation to the primary structures. Although the two lectins agglutinate tumor cells (e.g., Ehrlich, S-180 and AH109A ascites carcinoma cells), the liver RNase has no such activity. Agglutination of AH109A cells by the two lectins is inhibited by nucleotides. Our results indicate that the agglutination sites are not identical with, but are related to, the active sites of the three frog proteins.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a123457</identifier><identifier>PMID: 1917903</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Female ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Hydrogen-Ion Concentration ; Kinetics ; Lectins - chemistry ; Lectins - metabolism ; Liver - enzymology ; Molecular Sequence Data ; Ovum - metabolism ; Proteins ; Rana catesbeiana ; Rana japonica ; Ranidae ; Ribonucleases - chemistry ; Ribonucleases - metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Temperature</subject><ispartof>Journal of biochemistry (Tokyo), 1991-05, Vol.109 (5), p.786-790</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-6ff208ae6851330603da93f8a1152c7d22bd6b8fe6a0355ddb5131c4c08d2de93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4972258$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1917903$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okabe, Yukie</creatorcontrib><creatorcontrib>Katayama, Naoko</creatorcontrib><creatorcontrib>Iwama, Masanori</creatorcontrib><creatorcontrib>Watanabe, Hideaki</creatorcontrib><creatorcontrib>Ohgi, Kazuko</creatorcontrib><creatorcontrib>Irie, Masachika</creatorcontrib><creatorcontrib>Nitta, Kazuo</creatorcontrib><creatorcontrib>Kawauchi, Hiroaki</creatorcontrib><creatorcontrib>Takayanagi, Yoshio</creatorcontrib><creatorcontrib>Oyama, Fumitaka</creatorcontrib><creatorcontrib>Yasuko Abe, Koichl Titani</creatorcontrib><creatorcontrib>Okazaki, Taro</creatorcontrib><creatorcontrib>Inokuchi, Norio</creatorcontrib><creatorcontrib>Koyama, Takashi</creatorcontrib><title>Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The base specificities of the B1 and B2 sites of these proteins are U>C and G>U>A, C, respectively. The three frog proteins are more resistant than RNase A to heat treatment, guanidine-HCl and pH-induced denaturation; i.e.,they retain their native conformation up to at least 70°C at pH 7.5. Differences in stability and base specificity among RNase A and the three frog proteins are discussed in relation to the primary structures. Although the two lectins agglutinate tumor cells (e.g., Ehrlich, S-180 and AH109A ascites carcinoma cells), the liver RNase has no such activity. Agglutination of AH109A cells by the two lectins is inhibited by nucleotides. Our results indicate that the agglutination sites are not identical with, but are related to, the active sites of the three frog proteins.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Lectins - chemistry</subject><subject>Lectins - metabolism</subject><subject>Liver - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Ovum - metabolism</subject><subject>Proteins</subject><subject>Rana catesbeiana</subject><subject>Rana japonica</subject><subject>Ranidae</subject><subject>Ribonucleases - chemistry</subject><subject>Ribonucleases - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctu1DAUhi0EKtPCIyB5AazI4EviJAsW7VA6SIOQpgVVbKwTX4qHJA520sv78KAkzajAio3tc_7v_EfWj9ArSpaUlPytv7U-6J0fQgt1XO4q9d00S6CMp1n-CC1onomEiYw-RgtCGE1Kll4-RYcx7qaScX6ADmhJ85LwBfq18k0HAXp3bfAJRIPPO6Ocdcr1d2_weQ-Vq--f0Gq8Map3LT4ez-uxib3FFzd-347YBt_g06urOAlbaAEr6E2sjJvek8F2iXfQ-dapud6MawPeusq3g6rNtP_eZOT-Gn2Gntjxr-b5_j5CXz6cXqzWyebz2cfV8SZRvCz7RFjLSAFGFBnlnAjCNZTcFkBpxlSuGau0qAprBBCeZVpXI0dVqkihmTYlP0KvZ98u-J-Dib1sXFSmrqE1fogyZzSlOSX_BakglIh0cnw3gyr4GIOxsguugXAnKZFTnPLfOOUcp9zHOc6_2C8aqsboP9NzfqP-cq9DVFDbAK1y8QFLy5yxrBixZMZc7M3tgwzhhxQ5zzO5vvwm2ddP77f0ZC3P-G8W6MDy</recordid><startdate>199105</startdate><enddate>199105</enddate><creator>Okabe, Yukie</creator><creator>Katayama, Naoko</creator><creator>Iwama, Masanori</creator><creator>Watanabe, Hideaki</creator><creator>Ohgi, Kazuko</creator><creator>Irie, Masachika</creator><creator>Nitta, Kazuo</creator><creator>Kawauchi, Hiroaki</creator><creator>Takayanagi, Yoshio</creator><creator>Oyama, Fumitaka</creator><creator>Yasuko Abe, Koichl Titani</creator><creator>Okazaki, Taro</creator><creator>Inokuchi, Norio</creator><creator>Koyama, Takashi</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>199105</creationdate><title>Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana</title><author>Okabe, Yukie ; Katayama, Naoko ; Iwama, Masanori ; Watanabe, Hideaki ; Ohgi, Kazuko ; Irie, Masachika ; Nitta, Kazuo ; Kawauchi, Hiroaki ; Takayanagi, Yoshio ; Oyama, Fumitaka ; Yasuko Abe, Koichl Titani ; Okazaki, Taro ; Inokuchi, Norio ; Koyama, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-6ff208ae6851330603da93f8a1152c7d22bd6b8fe6a0355ddb5131c4c08d2de93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lectins - chemistry</topic><topic>Lectins - metabolism</topic><topic>Liver - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Ovum - metabolism</topic><topic>Proteins</topic><topic>Rana catesbeiana</topic><topic>Rana japonica</topic><topic>Ranidae</topic><topic>Ribonucleases - chemistry</topic><topic>Ribonucleases - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okabe, Yukie</creatorcontrib><creatorcontrib>Katayama, Naoko</creatorcontrib><creatorcontrib>Iwama, Masanori</creatorcontrib><creatorcontrib>Watanabe, Hideaki</creatorcontrib><creatorcontrib>Ohgi, Kazuko</creatorcontrib><creatorcontrib>Irie, Masachika</creatorcontrib><creatorcontrib>Nitta, Kazuo</creatorcontrib><creatorcontrib>Kawauchi, Hiroaki</creatorcontrib><creatorcontrib>Takayanagi, Yoshio</creatorcontrib><creatorcontrib>Oyama, Fumitaka</creatorcontrib><creatorcontrib>Yasuko Abe, Koichl Titani</creatorcontrib><creatorcontrib>Okazaki, Taro</creatorcontrib><creatorcontrib>Inokuchi, Norio</creatorcontrib><creatorcontrib>Koyama, Takashi</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okabe, Yukie</au><au>Katayama, Naoko</au><au>Iwama, Masanori</au><au>Watanabe, Hideaki</au><au>Ohgi, Kazuko</au><au>Irie, Masachika</au><au>Nitta, Kazuo</au><au>Kawauchi, Hiroaki</au><au>Takayanagi, Yoshio</au><au>Oyama, Fumitaka</au><au>Yasuko Abe, Koichl Titani</au><au>Okazaki, Taro</au><au>Inokuchi, Norio</au><au>Koyama, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1991-05</date><risdate>1991</risdate><volume>109</volume><issue>5</issue><spage>786</spage><epage>790</epage><pages>786-790</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The base specificities of the B1 and B2 sites of these proteins are U>C and G>U>A, C, respectively. The three frog proteins are more resistant than RNase A to heat treatment, guanidine-HCl and pH-induced denaturation; i.e.,they retain their native conformation up to at least 70°C at pH 7.5. Differences in stability and base specificity among RNase A and the three frog proteins are discussed in relation to the primary structures. Although the two lectins agglutinate tumor cells (e.g., Ehrlich, S-180 and AH109A ascites carcinoma cells), the liver RNase has no such activity. Agglutination of AH109A cells by the two lectins is inhibited by nucleotides. Our results indicate that the agglutination sites are not identical with, but are related to, the active sites of the three frog proteins.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>1917903</pmid><doi>10.1093/oxfordjournals.jbchem.a123457</doi><tpages>5</tpages></addata></record> |
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| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry; Oxford University Press Journals Digital Archive Legacy |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Female Fundamental and applied biological sciences. Psychology Glycoproteins Hydrogen-Ion Concentration Kinetics Lectins - chemistry Lectins - metabolism Liver - enzymology Molecular Sequence Data Ovum - metabolism Proteins Rana catesbeiana Rana japonica Ranidae Ribonucleases - chemistry Ribonucleases - metabolism Sequence Homology, Nucleic Acid Substrate Specificity Temperature |
| title | Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana |
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