Abstract
Reversed-phase high-performance liquid chromatography (HPLC) was used to study and characterize the in vitro proteolytic processing of β-endorphin by twice-washed membrane homogenates. A high-resolution method, capable of separating over 30 different human β-endorphin-related fragments in a single analysis, was used to study the time course of production of specific, biologically active endorphin fragments by membrane-associated proteases. The results demonstrate that frozen (-37°C), postmortem human and rat brains are viable for processing studies and that metabolism proceeds similarly to that in fresh brain homogenates or slices. Significant differences were noted in the formation rates of putative neuroleptic peptides between sex- and age-matched postmortem brain tissues from controls versus postmortem brain tissues from neuropsychiatric patients or drug-treated animals. These data suggest that using HPLC to characterize neuropeptide processing in human or rat membrane-associated enzyme homogenates is both descriptive and quantitative and offers insight into the central regulation of neuropeptide metabolism.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 279-292 |
| Number of pages | 14 |
| Journal | Journal of Chromatography A |
| Volume | 327 |
| Issue number | C |
| DOIs | |
| State | Published - Jun 26 1985 |
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ASJC Scopus subject areas
- Analytical Chemistry
- Clinical Biochemistry
- Molecular Medicine
Cite this
High-performance liquid chromatographic analysis of in vitro central neuropeptide processing. / Davis, Thomas P; Culling-Berglund, Alison.
In: Journal of Chromatography A, Vol. 327, No. C, 26.06.1985, p. 279-292.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - High-performance liquid chromatographic analysis of in vitro central neuropeptide processing
AU - Davis, Thomas P
AU - Culling-Berglund, Alison
PY - 1985/6/26
Y1 - 1985/6/26
N2 - Reversed-phase high-performance liquid chromatography (HPLC) was used to study and characterize the in vitro proteolytic processing of β-endorphin by twice-washed membrane homogenates. A high-resolution method, capable of separating over 30 different human β-endorphin-related fragments in a single analysis, was used to study the time course of production of specific, biologically active endorphin fragments by membrane-associated proteases. The results demonstrate that frozen (-37°C), postmortem human and rat brains are viable for processing studies and that metabolism proceeds similarly to that in fresh brain homogenates or slices. Significant differences were noted in the formation rates of putative neuroleptic peptides between sex- and age-matched postmortem brain tissues from controls versus postmortem brain tissues from neuropsychiatric patients or drug-treated animals. These data suggest that using HPLC to characterize neuropeptide processing in human or rat membrane-associated enzyme homogenates is both descriptive and quantitative and offers insight into the central regulation of neuropeptide metabolism.
AB - Reversed-phase high-performance liquid chromatography (HPLC) was used to study and characterize the in vitro proteolytic processing of β-endorphin by twice-washed membrane homogenates. A high-resolution method, capable of separating over 30 different human β-endorphin-related fragments in a single analysis, was used to study the time course of production of specific, biologically active endorphin fragments by membrane-associated proteases. The results demonstrate that frozen (-37°C), postmortem human and rat brains are viable for processing studies and that metabolism proceeds similarly to that in fresh brain homogenates or slices. Significant differences were noted in the formation rates of putative neuroleptic peptides between sex- and age-matched postmortem brain tissues from controls versus postmortem brain tissues from neuropsychiatric patients or drug-treated animals. These data suggest that using HPLC to characterize neuropeptide processing in human or rat membrane-associated enzyme homogenates is both descriptive and quantitative and offers insight into the central regulation of neuropeptide metabolism.
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UR - http://www.scopus.com/inward/citedby.url?scp=0022432821&partnerID=8YFLogxK
U2 - 10.1016/S0021-9673(01)81657-5
DO - 10.1016/S0021-9673(01)81657-5
M3 - Article
C2 - 2411750
AN - SCOPUS:0022432821
VL - 327
SP - 279
EP - 292
JO - Journal of Chromatography
JF - Journal of Chromatography
SN - 0021-9673
IS - C
ER -