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Size

Size-exclusion chromatography separates proteins and peptides by size, also known as hydrodynamic diameter. Smaller proteins are able to enter the pores of the stationary phase, traveling a longer path to the detector, while larger proteins travel a shorter path without entering pores. This low-resolution technique can separate proteins that differ in molecular weight by about one order of magnitude, and can help determine protein structure under native conditions.

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Maísa Habenschus
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16 views

Size

Size-exclusion chromatography separates proteins and peptides by size, also known as hydrodynamic diameter. Smaller proteins are able to enter the pores of the stationary phase, traveling a longer path to the detector, while larger proteins travel a shorter path without entering pores. This low-resolution technique can separate proteins that differ in molecular weight by about one order of magnitude, and can help determine protein structure under native conditions.

Uploaded by

Maísa Habenschus
Copyright
© Attribution Non-Commercial (BY-NC)
We take content rights seriously. If you suspect this is your content, claim it here.
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Size-Exclusion Chromatography (SEC, GPC, or GFC)

Size-exclusion chromatography (SEC) is also known as gel permeation chromatography


(GPC) when organic solvents are used as mobile phase, or gel Iiltration chromatography
(GFC) when aqueous solvents are used. This chromatography method separates proteins
and peptides according to their size (or more accurately according to their
hydrodynamic diameter or hydrodynamic volume). Smaller proteins are able to enter the
pores oI the stationary phase, thus, have relatively long path to travel until reaching the
detector. Larger proteins cannot enter the pores, thus, have shorter path to travel and
elute out Iirst. The average residence time in the pores depends upon the eIIective size
oI the proteins. It is generally a low-resolution chromatography technique with base-line
separation possible iI the molecular weights oI the two proteins are about one order oI
magnitude diIIerent. It is also useIul Ior determining the tertiary structure and
quaternary structure oI puriIied proteins, especially since it can be carried out under
native solution conditions. Salt and organic modiIiers are oIten added to minimize
interaction oI proteins to the stationary phase so a true MW determination can be
achieved with a calibration curve.

S|ze Lxc|us|on Chromatography (GIC)
nacalal Cosmosll ulol120ll
nacalal Cosmosll ulol300ll*
Sepax Zenlx SLC (3um 100300A)
Sepax S81 SLC* (1001000A)
Sepax S81C SLC* (1001000A)
Sepax nanofllm SLC* (130930A)

http://www.columnex.com/proteins.php

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