High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown
HAEMOGLOBIN J CAPETOWN 1 is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake 2 the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar 2,3 . Compared with normal Hb A, both have increas...
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| Veröffentlicht in: | Nature (London) 1970-03, Vol.225 (5237), p.1042-1043 |
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| container_issue | 5237 |
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| container_title | Nature (London) |
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| creator | OGAWA, S. SHULMAN, R. G. KYNOCH, P. A. M. LEHMANN, H. |
| description | HAEMOGLOBIN J CAPETOWN
1
is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake
2
the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar
2,3
. Compared with normal Hb A, both have increased oxygen affinities, smaller “haem-haem” interactions, and alkaline Bohr effects which are approximately normal. The X-ray crystallography of oxyhaemoglobin at 2.8 Å resolution, shows that the residue α92 (FG4) is at the α1βb2 interface
4
. Perutz and H. L.
5
have pointed out that all known haemoglobin variants with alterations at the α1β2 interface have reduced “haem-haem” interaction. |
| doi_str_mv | 10.1038/2251042a0 |
| format | Article |
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1
is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake
2
the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar
2,3
. Compared with normal Hb A, both have increased oxygen affinities, smaller “haem-haem” interactions, and alkaline Bohr effects which are approximately normal. The X-ray crystallography of oxyhaemoglobin at 2.8 Å resolution, shows that the residue α92 (FG4) is at the α1βb2 interface
4
. Perutz and H. L.
5
have pointed out that all known haemoglobin variants with alterations at the α1β2 interface have reduced “haem-haem” interaction.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/2251042a0</identifier><identifier>PMID: 5416469</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Hemoglobins, Abnormal ; Humanities and Social Sciences ; letter ; Magnetic Resonance Spectroscopy ; multidisciplinary ; Oxygen ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 1970-03, Vol.225 (5237), p.1042-1043</ispartof><rights>Springer Nature Limited 1970</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c315t-72f6c800a6398d4139187fbe4023e9120ec017d91a5be6454c0005e29653e9cf3</citedby><cites>FETCH-LOGICAL-c315t-72f6c800a6398d4139187fbe4023e9120ec017d91a5be6454c0005e29653e9cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/2251042a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/2251042a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5416469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OGAWA, S.</creatorcontrib><creatorcontrib>SHULMAN, R. G.</creatorcontrib><creatorcontrib>KYNOCH, P. A. M.</creatorcontrib><creatorcontrib>LEHMANN, H.</creatorcontrib><title>High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>HAEMOGLOBIN J CAPETOWN
1
is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake
2
the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar
2,3
. Compared with normal Hb A, both have increased oxygen affinities, smaller “haem-haem” interactions, and alkaline Bohr effects which are approximately normal. The X-ray crystallography of oxyhaemoglobin at 2.8 Å resolution, shows that the residue α92 (FG4) is at the α1βb2 interface
4
. Perutz and H. L.
5
have pointed out that all known haemoglobin variants with alterations at the α1β2 interface have reduced “haem-haem” interaction.</description><subject>Amino Acid Sequence</subject><subject>Hemoglobins, Abnormal</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>multidisciplinary</subject><subject>Oxygen</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE9LwzAYh4Moc04PfgAhJ0Gh-iZN0_QoQ50yFfxzLmn6tnZ0yUxaxG9v58ZOnnJ4Hh7e_Ag5ZXDFIFbXnCcMBNewR8ZMpDISUqX7ZAzAVQQqlofkKIQFACQsFSMySgSTQmZjMp819Sd9xeDavmucpc-9aVF7-qRri11j_pjV1iB96_qywUBdRWcal65uXdFY-kineoWd-7bH5KDSbcCT7TshH3e379NZNH-5f5jezCMTs6SLUl5JowC0jDNVChZnTKVVgQJ4jBnjgAZYWmZMJwVKkQizPhx5JpOBmyqekPNNd-XdV4-hy5dNMNi22qLrQ66EUEM7G8SLjWi8C8Fjla98s9T-J2eQr5fLd8sN7tk22hdLLHfmdqqBX254GIit0ecL13s7_POf2C87NXQd</recordid><startdate>19700314</startdate><enddate>19700314</enddate><creator>OGAWA, S.</creator><creator>SHULMAN, R. G.</creator><creator>KYNOCH, P. A. M.</creator><creator>LEHMANN, H.</creator><general>Nature Publishing Group UK</general><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>7X8</scope></search><sort><creationdate>19700314</creationdate><title>High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown</title><author>OGAWA, S. ; SHULMAN, R. G. ; KYNOCH, P. A. M. ; LEHMANN, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-72f6c800a6398d4139187fbe4023e9120ec017d91a5be6454c0005e29653e9cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Amino Acid Sequence</topic><topic>Hemoglobins, Abnormal</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>multidisciplinary</topic><topic>Oxygen</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OGAWA, S.</creatorcontrib><creatorcontrib>SHULMAN, R. G.</creatorcontrib><creatorcontrib>KYNOCH, P. A. M.</creatorcontrib><creatorcontrib>LEHMANN, H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OGAWA, S.</au><au>SHULMAN, R. G.</au><au>KYNOCH, P. A. M.</au><au>LEHMANN, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1970-03-14</date><risdate>1970</risdate><volume>225</volume><issue>5237</issue><spage>1042</spage><epage>1043</epage><pages>1042-1043</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>HAEMOGLOBIN J CAPETOWN
1
is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake
2
the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar
2,3
. Compared with normal Hb A, both have increased oxygen affinities, smaller “haem-haem” interactions, and alkaline Bohr effects which are approximately normal. The X-ray crystallography of oxyhaemoglobin at 2.8 Å resolution, shows that the residue α92 (FG4) is at the α1βb2 interface
4
. Perutz and H. L.
5
have pointed out that all known haemoglobin variants with alterations at the α1β2 interface have reduced “haem-haem” interaction.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>5416469</pmid><doi>10.1038/2251042a0</doi><tpages>2</tpages></addata></record> |
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| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; SpringerNature Complete Journals |
| subjects | Amino Acid Sequence Hemoglobins, Abnormal Humanities and Social Sciences letter Magnetic Resonance Spectroscopy multidisciplinary Oxygen Science Science (multidisciplinary) |
| title | High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown |
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