Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Katherine C. Bechtel"'
Autor:
E. Brosious, Winston F. Moo-Penn, Robert M. Schmidt, E. Bemis, Katherine C. Bechtel, Mary H. Johnson, Danny L. Jue
Publikováno v:
Biochemical and Biophysical Research Communications. 65:8-15
Summary Hemoglobin Deaconess was detected as a band migrating in the position of fetal hemoglobin when an hemolyzate was electrophoresed on cellulose acetate at pH 8.4. This abnormal hemoglobin also migrates between Hb S and C on citrate agar electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c500964c588987eb283147744e140cc2
https://doi.org/10.1016/s0006-291x(75)80054-4
https://doi.org/10.1016/s0006-291x(75)80054-4
Publikováno v:
Hemoglobin. 1:233-244
Procedures are described for the preparation of cyanogen bromide and maleyl peptides of the alpha and beta chains of human hemoglobin. These relatively large peptides have facilitated application of automated sequencing techniques to determine mutati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::828949e1781a5616afbad04b23617626
https://doi.org/10.3109/03630267709003406
https://doi.org/10.3109/03630267709003406
Autor:
Robert M. Schmidt, Bradford L. Therrell, Katherine C. Bechtel, Winston F. Moo-Penn, Mary H. Johnson
Publikováno v:
Hemoglobin. 1:799-814
Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the beta chain. Marked instability of the variant hemoglobin is demonstrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5bfaec4b5702ea69a91236b8b8951c10
https://doi.org/10.3109/03630267709003908
https://doi.org/10.3109/03630267709003908
Autor:
C. Huff, Winston F. Moo-Penn, Katherine C. Bechtel, S. Holland, Robert M. Schmidt, Mary H. Johnson, Danny L. Jue
Publikováno v:
American Journal of Clinical Pathology. 66:453-456
A new hemoglobin mutant was detected as a fast-moving variant on cellulose acetate electrophoresis at pH 8.4. The mutation is in the alpha-chain at position 127, where lysine is substituted by asparagine. This is an external residue, and mutation at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3402664b2ff8af05acada4e11084955b
https://doi.org/10.1093/ajcp/66.2.453
https://doi.org/10.1093/ajcp/66.2.453
Publikováno v:
Journal of Chromatography A. 172:476-480
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1be1ddac58e1b6896d1e16490621159c
https://doi.org/10.1016/s0021-9673(00)91001-x
https://doi.org/10.1016/s0021-9673(00)91001-x
Autor:
Katherine C. Bechtel, Danny L. Jue, Jane M. Wright, Winston F. Moo-Penn, M. S. Chan, G. Hopkins, Robert M. Schmidt, N. J. Schneider
Publikováno v:
Blood. 46:363-367
The first reported case of hemoglobin S and C Harlem in an individual is described. The patient, a 35-yr-old female, had numerous crises during adolescence and early adulthood, but these occurred more infrequently as she grew older. Chemical evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6913010998c9820aaf7686e7a321d3c7
https://doi.org/10.1182/blood.v46.3.363.bloodjournal463363
https://doi.org/10.1182/blood.v46.3.363.bloodjournal463363
Autor:
McDonald K. Horne, Ronald L. Nagel, Winston F. Moo-Penn, Eugene F. Roth, Danny L. Jue, Robert M. Schmidt, Jane M. Wright, Gordon L. Haycraft, Katherine C. Bechtel
Publikováno v:
European Journal of Biochemistry. 77:561-566
Hb S Travis is a previously undescribed sickling hemoglobin with two amino acid substitutions in the p chain: p6 Glu-Val and p142 Ala-tVal. The p6 Glu-Val mutation imparts to HbS Travis the characteristic properties of sickling hemoglobin, namely its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::411f190d764bdb64d4040664525167df
https://doi.org/10.1111/j.1432-1033.1977.tb11699.x
https://doi.org/10.1111/j.1432-1033.1977.tb11699.x
Publikováno v:
Hemoglobin. 2:65-69
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f87cb7a0f85e308f3b7b6581260593db
https://doi.org/10.3109/03630267808999190
https://doi.org/10.3109/03630267808999190
Publikováno v:
Journal of Biological Chemistry. 251:7557-7562
Hemoglobin Providence Asn and Hemoglobin Providence Asp are two abnormal hemoglobins which apparently arise from a single genetic change that substitutes asparagine for lysine at position 82 (EF6) in the beta chain of human hemoglobin.The second form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1be9d2a2178eff048a30c79be76fecf
https://doi.org/10.1016/s0021-9258(17)32887-9
https://doi.org/10.1016/s0021-9258(17)32887-9
Autor:
Babara Hightower, Mary H. Johnson, Rose G. Schneider, D.K. Das, Winston F. Moo-Penn, S. Andrian, Katherine C. Bechtel, Danny L. Jue
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 536:283-288
Hb Detroit is a mutant which migrates between Hb A and Hb J Baltimore on cellulose acetate (pH 8.5),and with Hb A on citrate agar (pH 6.0). Globin chain analyses in alkaline and acid buffers reveal an abnormal β chain with a mobility between the βA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6d22eb04d7a3d688a5c50c2a9779f7b
https://doi.org/10.1016/0005-2795(78)90075-2
https://doi.org/10.1016/0005-2795(78)90075-2