Abstract
Cross-linking of the protein with bifunctional reagents offers the prospects of stabilizing various functional states and thus clarifying the structure-function relationship. This approach has been applied to other enzymes of a similar nature.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 569-577 |
| Number of pages | 9 |
| Journal | Methods |
| Volume | 135 |
| State | Published - 1987 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
Cite this
Chemical stabilization of conformational states of aspartate transcarbamoylase. / Enns, Caroline; Chan, W. W C.
In: Methods, Vol. 135, 1987, p. 569-577.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Chemical stabilization of conformational states of aspartate transcarbamoylase
AU - Enns, Caroline
AU - Chan, W. W C
PY - 1987
Y1 - 1987
N2 - Cross-linking of the protein with bifunctional reagents offers the prospects of stabilizing various functional states and thus clarifying the structure-function relationship. This approach has been applied to other enzymes of a similar nature.
AB - Cross-linking of the protein with bifunctional reagents offers the prospects of stabilizing various functional states and thus clarifying the structure-function relationship. This approach has been applied to other enzymes of a similar nature.
UR - http://www.scopus.com/inward/record.url?scp=0023606683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023606683&partnerID=8YFLogxK
M3 - Article
VL - 135
SP - 569
EP - 577
JO - ImmunoMethods
JF - ImmunoMethods
SN - 1046-2023
ER -