Journal article
Growth hormone heterogeneity in American plaice pituitaries: Isolation, characterization, and partial amino acid sequence
General and comparative endocrinology, Vol.84(3), pp.365-373
1991
Handle:
https://hdl.handle.net/2376/106605
PMID: 1808017
Abstract
Growth hormones (GHs) have been isolated from pituitary glands of American plaice (
Hippoglossoides platessoides), a marine flatfish, using affinity and gel filtration chromatography, followed by preparative polyacrylamide gel electrophoresis (PAGE). A bioassay based on serum triiodothyronine elevation in immature rainbow trout was used to monitor biological activity. These GHs originate from two molecular mass regions, 42K and < 33K relative molecular mass (
M
r), in their native state. The 42K
M
r region yielded two forms of GH, which differ in terms of quantity and net charge as evidenced by native PAGE, a major variant with a relative mobility of (
R
f) 0.22 and a lesser variant with
R
f 0.28. The <33
M
r region has a single GH species with
R
f 0.22. Upon sodium dodecyl sulfate-PAGE, without reduction, both GH variants from the 42K
M
r region gave
M
rs of 21K, while the GH from the <33K
M
r region was 20K
M
r, typical of monomeric vertebrate GHs. The proteins composing the 42K
M
r region are proposed as GH dimers since they yield 21K
M
r peptides. The <33K
M
r region contains a GH monomer (20K
M
r) in its native state. An aminoterminal amino acid sequence, identical for both the 42K and the 20K
M
r,
R
f 0.22 forms, has good homology with other complete fish GH sequences near their carboxyl-terminal regions (between amino acids 130 and 196). The GH dimers (42K
M
r) predominate in the plaice pituitary, contributing 93% of the total, of which 86% gives rise to the
R
f 0.22 variant.
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Details
- Title
- Growth hormone heterogeneity in American plaice pituitaries: Isolation, characterization, and partial amino acid sequence
- Creators
- James J NaglerShinn Jia HwangDavid R Idler
- Publication Details
- General and comparative endocrinology, Vol.84(3), pp.365-373
- Academic Unit
- UNKNOWN
- Publisher
- Elsevier Inc
- Identifiers
- 99900546995201842
- Language
- English
- Resource Type
- Journal article