Stability of rat pituitary gonadotropins during nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Brooks Allen Keel, H. E. Grotjan

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

I-(rLH) and 125I-(rFSH) were dissolved in sample buffer containing 0-0.1 % (SDS) and subjected to SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions at room temperature. 125I-rFSH migrated as a single band, while 125I-rLH migrated as two bands corresponding to rLH and rLH subunits suggesting partial dissociation. The dissociation of rLH increased as the concentration of SDS in the sample buffer was increased. However, electrophoresis of 125I-rLH at 4°C under nonreducing conditions caused minimal dissociation. These data suggest that (1) substantial dissociation of rLH, but not rFSH, occurs during nonreducing SDS-PAGE at room temperature and (2) running the gels at 4°C minimizes the dissociation of rLH.

Original languageEnglish (US)
Pages (from-to)207-214
Number of pages8
JournalSystems Biology in Reproductive Medicine
Volume17
Issue number3
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

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Pituitary Gonadotropins
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Buffers
Temperature
Running
Electrophoresis
Gels

Keywords

  • Electrophoresis
  • Gonadotropins
  • Pituitary
  • Rat

ASJC Scopus subject areas

  • Reproductive Medicine
  • Urology

Cite this

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title = "Stability of rat pituitary gonadotropins during nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis",
abstract = "I-(rLH) and 125I-(rFSH) were dissolved in sample buffer containing 0-0.1 {\%} (SDS) and subjected to SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions at room temperature. 125I-rFSH migrated as a single band, while 125I-rLH migrated as two bands corresponding to rLH and rLH subunits suggesting partial dissociation. The dissociation of rLH increased as the concentration of SDS in the sample buffer was increased. However, electrophoresis of 125I-rLH at 4°C under nonreducing conditions caused minimal dissociation. These data suggest that (1) substantial dissociation of rLH, but not rFSH, occurs during nonreducing SDS-PAGE at room temperature and (2) running the gels at 4°C minimizes the dissociation of rLH.",
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N2 - I-(rLH) and 125I-(rFSH) were dissolved in sample buffer containing 0-0.1 % (SDS) and subjected to SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions at room temperature. 125I-rFSH migrated as a single band, while 125I-rLH migrated as two bands corresponding to rLH and rLH subunits suggesting partial dissociation. The dissociation of rLH increased as the concentration of SDS in the sample buffer was increased. However, electrophoresis of 125I-rLH at 4°C under nonreducing conditions caused minimal dissociation. These data suggest that (1) substantial dissociation of rLH, but not rFSH, occurs during nonreducing SDS-PAGE at room temperature and (2) running the gels at 4°C minimizes the dissociation of rLH.

AB - I-(rLH) and 125I-(rFSH) were dissolved in sample buffer containing 0-0.1 % (SDS) and subjected to SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions at room temperature. 125I-rFSH migrated as a single band, while 125I-rLH migrated as two bands corresponding to rLH and rLH subunits suggesting partial dissociation. The dissociation of rLH increased as the concentration of SDS in the sample buffer was increased. However, electrophoresis of 125I-rLH at 4°C under nonreducing conditions caused minimal dissociation. These data suggest that (1) substantial dissociation of rLH, but not rFSH, occurs during nonreducing SDS-PAGE at room temperature and (2) running the gels at 4°C minimizes the dissociation of rLH.

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