Analysis of intact protein isoforms by mass spectrometry

Jeremiah D. Tipton; John C. Tran; Adam D. Catherman; Dorothy R. Ahlf; Kenneth R. Durbin; Neil L. Kelleher

doi:10.1074/jbc.R111.239442

Analysis of intact protein isoforms by mass spectrometry

Jeremiah D. Tipton, John C. Tran, Adam D. Catherman, Dorothy R. Ahlf, Kenneth R. Durbin, Neil L. Kelleher^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Short survey › peer-review

87 Scopus citations

Abstract

The diverse proteome of an organism arises from such events as single nucleotide substitutions at the DNA level, different RNA processing, and dynamic enzymatic post-translational modifications. This minireview focuses on the measurement of intact proteins to describe the diversity found in proteomes. The field of biological mass spectrometry has steadily advanced, enabling improvements in the characterization of single proteins to proteins derived from cells or tissues. In this minireview, we discuss the basic technology for "top-down" intact protein analysis. Furthermore, examples of studies involved with the qualitative and quantitative analysis of full-length polypeptides are provided.

Original language	English (US)
Pages (from-to)	25451-25458
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	286
Issue number	29
DOIs	https://doi.org/10.1074/jbc.R111.239442
State	Published - Jul 22 2011

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

Access to Document

10.1074/jbc.R111.239442

Cite this

@article{ba6c9d9f4d074c3fa69ccfd661d72a00,

title = "Analysis of intact protein isoforms by mass spectrometry",

abstract = "The diverse proteome of an organism arises from such events as single nucleotide substitutions at the DNA level, different RNA processing, and dynamic enzymatic post-translational modifications. This minireview focuses on the measurement of intact proteins to describe the diversity found in proteomes. The field of biological mass spectrometry has steadily advanced, enabling improvements in the characterization of single proteins to proteins derived from cells or tissues. In this minireview, we discuss the basic technology for {"}top-down{"} intact protein analysis. Furthermore, examples of studies involved with the qualitative and quantitative analysis of full-length polypeptides are provided.",

author = "Tipton, {Jeremiah D.} and Tran, {John C.} and Catherman, {Adam D.} and Ahlf, {Dorothy R.} and Durbin, {Kenneth R.} and Kelleher, {Neil L.}",

year = "2011",

month = jul,

day = "22",

doi = "10.1074/jbc.R111.239442",

language = "English (US)",

volume = "286",

pages = "25451--25458",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "29",

}

TY - JOUR

T1 - Analysis of intact protein isoforms by mass spectrometry

AU - Tipton, Jeremiah D.

AU - Tran, John C.

AU - Catherman, Adam D.

AU - Ahlf, Dorothy R.

AU - Durbin, Kenneth R.

AU - Kelleher, Neil L.

PY - 2011/7/22

Y1 - 2011/7/22

N2 - The diverse proteome of an organism arises from such events as single nucleotide substitutions at the DNA level, different RNA processing, and dynamic enzymatic post-translational modifications. This minireview focuses on the measurement of intact proteins to describe the diversity found in proteomes. The field of biological mass spectrometry has steadily advanced, enabling improvements in the characterization of single proteins to proteins derived from cells or tissues. In this minireview, we discuss the basic technology for "top-down" intact protein analysis. Furthermore, examples of studies involved with the qualitative and quantitative analysis of full-length polypeptides are provided.

AB - The diverse proteome of an organism arises from such events as single nucleotide substitutions at the DNA level, different RNA processing, and dynamic enzymatic post-translational modifications. This minireview focuses on the measurement of intact proteins to describe the diversity found in proteomes. The field of biological mass spectrometry has steadily advanced, enabling improvements in the characterization of single proteins to proteins derived from cells or tissues. In this minireview, we discuss the basic technology for "top-down" intact protein analysis. Furthermore, examples of studies involved with the qualitative and quantitative analysis of full-length polypeptides are provided.

UR - http://www.scopus.com/inward/record.url?scp=79960415849&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960415849&partnerID=8YFLogxK

U2 - 10.1074/jbc.R111.239442

DO - 10.1074/jbc.R111.239442

M3 - Short survey

C2 - 21632550

AN - SCOPUS:79960415849

SN - 0021-9258

VL - 286

SP - 25451

EP - 25458

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 29

ER -

Analysis of intact protein isoforms by mass spectrometry

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this