Biological characterization of purified native 20-kDa human growth hormone
dc.contributor.author | Kostyo, Jack L. | en_US |
dc.contributor.author | Skottner, Anna | en_US |
dc.contributor.author | Brostedt, Peter | en_US |
dc.contributor.author | Roos, Paul | en_US |
dc.contributor.author | Cameron, Christopher M. | en_US |
dc.contributor.author | Forsman, Anders | en_US |
dc.contributor.author | Fryklund, Linda | en_US |
dc.contributor.author | Adamafio, Naa A. | en_US |
dc.contributor.author | Skoog, Bo | en_US |
dc.date.accessioned | 2006-04-07T19:48:34Z | |
dc.date.available | 2006-04-07T19:48:34Z | |
dc.date.issued | 1987-09-11 | en_US |
dc.identifier.citation | Kostyo, Jack L., Skottner, Anna, Brostedt, Peter, Roos, Paul, Cameron, Christopher M., Forsman, Anders, Fryklund, Linda, Adamafio, Naa A., Skoog, Bo (1987/09/11)."Biological characterization of purified native 20-kDa human growth hormone." Biochimica et Biophysica Acta (BBA) - General Subjects 925(3): 314-324. <http://hdl.handle.net/2027.42/26576> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1W-47MCSYX-XX/2/9c66762e0e90e8986a228dd148b03b76 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/26576 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3620504&dopt=citation | en_US |
dc.description.abstract | Because of the propensity of the 20-kDa variant of human growth human (GH) to aggregate with itself and with 22-kDa human GH, it has been difficult to prepare monomeric 20-kDa GH in highly purified form. This has been a major complicating factor in determining whether 20-kDa GH has a biological activity profile distinct from that of 22-kDa GH. In the present study, native 20-kDa GH was isolated from a human GH dimer concentrate and purified by a procedure that included column electrophoresis in agarose suspension as a final separation step. This procedure yielded highly purified monomeric 20-kDa GH, which was contaminated to an extent of less than 1% with 22-kDa GH, and which exhibited only a small degree of dimerization upon storage. The native 20-kDa Gh was quite active in stimulating growth in hypophysectomized rats, when growth was assessed by body weight gain, longitudinal bone growth, the stimulation of sulfation of cartilage, and the elevation of serum IGF-1 level. However, in all of these growth assays, the 20-kDa GH was somewhat less active than the native 22-kDa GH to which it was compared; e.g., in the body weight gain and longitudinal bone growth assays, it had an estimated potency of 0.6 relative to the 22-kDa GH. The 20-kDa GH exhibited substantial diabetogenic activity when tested for the ability to raise fasting blood glucose concentration and to impair glucose tolerance in ob/ob mice. Also, the native 20-kDa GH had significant in vitro insulin-like activity, although its potency was approximately 20% that of the native 22-kDa GH to which it was compared. Thus, the biological activity profile of native 20-kDa GH differs from that of 22-kDa GH primarily in that insulin-like activity is markedly attenuated. | en_US |
dc.format.extent | 1022808 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Biological characterization of purified native 20-kDa human growth hormone | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Physiology, The University of Michigan Medical School, Ann Arbor, MI, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Physiology, The University of Michigan Medical School, Ann Arbor, MI, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Physiology, The University of Michigan Medical School, Ann Arbor, MI, U.S.A. | en_US |
dc.contributor.affiliationother | KabiVitrum AB, Stockholm, Sweden | en_US |
dc.contributor.affiliationother | Department of Biochemistry, University of Uppsala, Uppsala, Sweden | en_US |
dc.contributor.affiliationother | Department of Biochemistry, University of Uppsala, Uppsala, Sweden | en_US |
dc.contributor.affiliationother | KabiVitrum AB, Stockholm, Sweden | en_US |
dc.contributor.affiliationother | KabiVitrum AB, Stockholm, Sweden | en_US |
dc.contributor.affiliationother | KabiVitrum AB, Stockholm, Sweden | en_US |
dc.identifier.pmid | 3620504 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/26576/1/0000115.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0304-4165(87)90197-8 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.