The use of plasma desorption time-of-flight mass spectrometry to screen for products of prohormone processing in crude tissue extracts

P. C. Andrews; Mershid Alai; Robert J. Cotter

doi:10.1016/0003-2697(88)90514-3

The use of plasma desorption time-of-flight mass spectrometry to screen for products of prohormone processing in crude tissue extracts

P. C. Andrews, Mershid Alai, Robert J. Cotter

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Californium-252 plasma desorption mass spectrometry (²⁵²Cf PDMS) of a crude, desalted, extract of piscine endocrine pancreas provided mass information for the major biologically active peptide hormones present in this tissue. An extraction procedure compatible with ²⁵²Cf PDMS analysis was developed. In extracts of catfish pancreas, strong molecular ions were identified in the positive mode for somatostatin-14 (1638 amu), O-glycosylated somatostatin-22 (2944 amu), glucagon (3512 amu), glucagon-like peptide (3785 amu), insulin (ca. 5550 amu), and other prohormone-derived peptides. Both protonated species and sodium adducts were apparent in the mass spectrum. A number of other molecular ions were observed including somatostatin-26, 1-10 (1014 amu) and the entire portion of prosomatostatin-22 remaining after removal of somatostatin-22 (6465 amu). The data obtained by this method also resulted in the identification of the third major product of proglucagon processing in catfish pancreas, glicentin-related polypeptide. Subtractive Edman degradation analyzed by ²⁵²Cf PDMS was also used to confirm a mass assignment.

Original language	English (US)
Pages (from-to)	23-31
Number of pages	9
Journal	Analytical biochemistry
Volume	174
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(88)90514-3
State	Published - Oct 1988
Externally published	Yes

Keywords

diabetes
glucagon
pancreas
peptide hormones
plasma desorption
time-of-flight

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0003-2697(88)90514-3

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title = "The use of plasma desorption time-of-flight mass spectrometry to screen for products of prohormone processing in crude tissue extracts",

abstract = "Californium-252 plasma desorption mass spectrometry (252Cf PDMS) of a crude, desalted, extract of piscine endocrine pancreas provided mass information for the major biologically active peptide hormones present in this tissue. An extraction procedure compatible with 252Cf PDMS analysis was developed. In extracts of catfish pancreas, strong molecular ions were identified in the positive mode for somatostatin-14 (1638 amu), O-glycosylated somatostatin-22 (2944 amu), glucagon (3512 amu), glucagon-like peptide (3785 amu), insulin (ca. 5550 amu), and other prohormone-derived peptides. Both protonated species and sodium adducts were apparent in the mass spectrum. A number of other molecular ions were observed including somatostatin-26, 1-10 (1014 amu) and the entire portion of prosomatostatin-22 remaining after removal of somatostatin-22 (6465 amu). The data obtained by this method also resulted in the identification of the third major product of proglucagon processing in catfish pancreas, glicentin-related polypeptide. Subtractive Edman degradation analyzed by 252Cf PDMS was also used to confirm a mass assignment.",

keywords = "diabetes, glucagon, pancreas, peptide hormones, plasma desorption, time-of-flight",

author = "Andrews, {P. C.} and Mershid Alai and Cotter, {Robert J.}",

note = "Funding Information: The authors thank Dr. M. Hermodson, Purdue University, for sequence analysis. J. E. Dixon and F. Regnier, Purdue University. are also thanked for helpful discussions. P. C. Andrews thanks J. E. Hoover for helpful discussions. This project was supported in part by NIH Grant AM18849. P. C. Andrews was supported by a grant from the American Diabetes Association and M. Alai by the Fonds FCAR (Canada). Mass spectral measurements were supported by Grants DMB 85-15390 from the National Science Foundation and RR-02727 from the National Institutes of Health. Measurements were carried out at the Middle Atlantic Mass Spectrometry Facility, an NSF shared instrumentation facility. This study was supported, in part, by NSF Grant ECE86 13 167.",

year = "1988",

month = oct,

doi = "10.1016/0003-2697(88)90514-3",

language = "English (US)",

volume = "174",

pages = "23--31",

journal = "Analytical biochemistry",

issn = "0003-2697",

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T1 - The use of plasma desorption time-of-flight mass spectrometry to screen for products of prohormone processing in crude tissue extracts

AU - Andrews, P. C.

AU - Alai, Mershid

AU - Cotter, Robert J.

N1 - Funding Information: The authors thank Dr. M. Hermodson, Purdue University, for sequence analysis. J. E. Dixon and F. Regnier, Purdue University. are also thanked for helpful discussions. P. C. Andrews thanks J. E. Hoover for helpful discussions. This project was supported in part by NIH Grant AM18849. P. C. Andrews was supported by a grant from the American Diabetes Association and M. Alai by the Fonds FCAR (Canada). Mass spectral measurements were supported by Grants DMB 85-15390 from the National Science Foundation and RR-02727 from the National Institutes of Health. Measurements were carried out at the Middle Atlantic Mass Spectrometry Facility, an NSF shared instrumentation facility. This study was supported, in part, by NSF Grant ECE86 13 167.

PY - 1988/10

Y1 - 1988/10

N2 - Californium-252 plasma desorption mass spectrometry (252Cf PDMS) of a crude, desalted, extract of piscine endocrine pancreas provided mass information for the major biologically active peptide hormones present in this tissue. An extraction procedure compatible with 252Cf PDMS analysis was developed. In extracts of catfish pancreas, strong molecular ions were identified in the positive mode for somatostatin-14 (1638 amu), O-glycosylated somatostatin-22 (2944 amu), glucagon (3512 amu), glucagon-like peptide (3785 amu), insulin (ca. 5550 amu), and other prohormone-derived peptides. Both protonated species and sodium adducts were apparent in the mass spectrum. A number of other molecular ions were observed including somatostatin-26, 1-10 (1014 amu) and the entire portion of prosomatostatin-22 remaining after removal of somatostatin-22 (6465 amu). The data obtained by this method also resulted in the identification of the third major product of proglucagon processing in catfish pancreas, glicentin-related polypeptide. Subtractive Edman degradation analyzed by 252Cf PDMS was also used to confirm a mass assignment.

AB - Californium-252 plasma desorption mass spectrometry (252Cf PDMS) of a crude, desalted, extract of piscine endocrine pancreas provided mass information for the major biologically active peptide hormones present in this tissue. An extraction procedure compatible with 252Cf PDMS analysis was developed. In extracts of catfish pancreas, strong molecular ions were identified in the positive mode for somatostatin-14 (1638 amu), O-glycosylated somatostatin-22 (2944 amu), glucagon (3512 amu), glucagon-like peptide (3785 amu), insulin (ca. 5550 amu), and other prohormone-derived peptides. Both protonated species and sodium adducts were apparent in the mass spectrum. A number of other molecular ions were observed including somatostatin-26, 1-10 (1014 amu) and the entire portion of prosomatostatin-22 remaining after removal of somatostatin-22 (6465 amu). The data obtained by this method also resulted in the identification of the third major product of proglucagon processing in catfish pancreas, glicentin-related polypeptide. Subtractive Edman degradation analyzed by 252Cf PDMS was also used to confirm a mass assignment.

KW - diabetes

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KW - plasma desorption

KW - time-of-flight

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The use of plasma desorption time-of-flight mass spectrometry to screen for products of prohormone processing in crude tissue extracts

Abstract

Keywords

ASJC Scopus subject areas

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