Zobrazeno 1 - 10
of 19
pro vyhledávání: '"B N Manjula"'
Publikováno v:
International Journal of Peptide and Protein Research. 8:275-282
A study has been made on the changes in the enzymatic activity of Ribonuclease-A**-(RNase-A) exposed to highly acidic (pH less than 1) acqueous environment. Irreversible alterations of activity were observed when the protein was exposed to an acidic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99cd0abac0d5e53ff5763674a3b1bb77
https://doi.org/10.1111/j.1399-3011.1976.tb02504.x
https://doi.org/10.1111/j.1399-3011.1976.tb02504.x
Publikováno v:
Diabetes. 45:1694-1700
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a2b036f78ca71229829b7b3fccf9dbf
https://doi.org/10.2337/diabetes.45.12.1694
https://doi.org/10.2337/diabetes.45.12.1694
Autor:
J Okabe, C Adams, K Sundarapandiyan, S P White, A S Acharya, C T Parsons, Michael J. Martin, B N Manjula, Patrick Birch, J K O'Donnell
Publikováno v:
Journal of Biological Chemistry. 269:27692-27699
Hemoglobin A (HbA) and two low oxygen affinity variants of HbA, HbPresbyterian and HbYoshizuka, were produced in transgenic pigs and purified to homogeneity by ion-exchange chromatography. These two variants contain either lysine (HbPresbyterian) or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a126690412c4209fc01e318b9696c7cb
https://doi.org/10.1016/s0021-9258(18)47041-x
https://doi.org/10.1016/s0021-9258(18)47041-x
Autor:
Ramesh Kumar, Klaus Schneider, H Keller, B N Manjula, T L Chao, M J Rao, A. S. Acharya, Brian T. Chait, S Anderson
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 22:695-700
Recombinant human hemoglobin A produced by coexpressing human alpha and beta globin genes in swine, and purified from the lysate of transgenic swine has been subjected to detailed protein chemical analysis. These structural studies involving laser de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba85e34d6da9d9a5eff92d7ee9e613fe
https://doi.org/10.3109/10731199409117900
https://doi.org/10.3109/10731199409117900
Publikováno v:
Infection and Immunity. 61:3703-3710
The important human pathogens Neisseria meningitidis and Neisseria gonorrhoeae accumulate phosphate in the form of polyphosphate (A. Noegel and E. C. Gotschlich, J. Exp. Med. 157:2049-2060, 1983), and the localization of more than half of this long-c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8c876f660bd266868a75ae8e8cbb4b2
https://doi.org/10.1128/iai.61.9.3703-3710.1993
https://doi.org/10.1128/iai.61.9.3703-3710.1993
Publikováno v:
The Journal of biological chemistry. 275(8)
Bis(maleidophenyl)-PEG2000 (Bis-Mal-PEG2000), a new bifunctional protein cross-linker targeted to sulfhydryl groups, introduces intra-tetrameric cross-links into oxy-HbA in nearly quantitative yields. Structural as well as crystallographic analyses o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eb07677081f629eb8f8d0e9a7df31ea0
https://pubmed.ncbi.nlm.nih.gov/10681532
https://pubmed.ncbi.nlm.nih.gov/10681532
Autor:
V A Fischetti, B N Manjula
Publikováno v:
The Journal of Experimental Medicine
Partial sequences of three immunologically distinct group A streptococcal M proteins (M5, M6, and M24) revealed significant homology with each other, certain amino acid residues being conserved within the three molecules. In addition, a common featur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ff0f9f60b631df9b3be13d34951db69
https://doi.org/10.1084/jem.151.3.695
https://doi.org/10.1084/jem.151.3.695
Publikováno v:
Biochemical Journal. 165:337-345
Limited proteolysis of RNAase-Aa(1) (monodeamidated ribonuclease-A) by subtilisin results in the formation of an active RNAase-S type of derivative, namely RNAase-Aa(1)S. RNAase-Aa(1)S was chromatographically distinct from RNAase-S, but exhibited ver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5a003b68cc8b94a0299e6942418bda0
https://doi.org/10.1042/bj1650337
https://doi.org/10.1042/bj1650337
Structure and enzymic activity of ribonuclease-A esterified at glutamic acid-49 and aspartic acid-53
Publikováno v:
Biochemical Journal. 173:821-830
The dimethyl ester of bovine pancreatic ribonuclease-A (dimethyl RNAase-A), the initial product of esterification of RNAase-A in anhydrous methanolic HCl, was isolated in a homogeneous form. The two carboxy functions esterified in this derivative are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fe5fb423fcb71d2049b171142df3356
https://doi.org/10.1042/bj1730821
https://doi.org/10.1042/bj1730821
Publikováno v:
Biochemistry. 27:4522-4529
Nonreductive modification of proteins with glyceraldehyde forming 2-oxo-3-hydroxypropylated protein is mechanistically analogous to nonenzymic glycation reactions. The latent cross-linking potential of glyceraldehyde as a consequence of the reactivit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84d1dc474a14dfc33b4424dd64f150c4
https://doi.org/10.1021/bi00412a045
https://doi.org/10.1021/bi00412a045