Single alkaline phosphatase molecule assay by capillary electrophoresis laser-induced fluorescence detection

Douglas B. Craig; Edgar A. Arriaga; Jerome C.Y. Wong; Hui Lu; Norman J. Dovichi

doi:10.1016/S1080-8914(97)80015-4

Single alkaline phosphatase molecule assay by capillary electrophoresis laser-induced fluorescence detection

Douglas B. Craig, Edgar A. Arriaga, Jerome C.Y. Wong, Hui Lu, Norman J. Dovichi

Chemistry (Twin Cities)

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

1 Scopus citations

Abstract

Single molecules of alkaline phosphatase were assayed using capillary electrophoresis laser-induced fluorescence detection. Multiple incubations of individual molecules were performed. Varying the temperature in multiple incubation assay allowed for the determination of the activation energy of catalysis at the single molecule level. Molecules are heterogeneous with respect to both activity and activation energy of catalysis. Partial thermal denaturation of alkaline phosphatase results from the total denaturation of a fraction of the molecules with surviving molecules unaffected rather than a partial decrease in the activity of all the molecules.

Original language	English (US)
Pages (from-to)	121-131
Number of pages	11
Journal	Techniques in Protein Chemistry
Volume	8
Issue number	C
DOIs	https://doi.org/10.1016/S1080-8914(97)80015-4
State	Published - Dec 1 1997

Access

10.1016/S1080-8914(97)80015-4

Fingerprint Dive into the research topics of 'Single alkaline phosphatase molecule assay by capillary electrophoresis laser-induced fluorescence detection'. Together they form a unique fingerprint.

Cite this

@article{a358b9eba0ba4d189c740710fce733c4,

title = "Single alkaline phosphatase molecule assay by capillary electrophoresis laser-induced fluorescence detection",

abstract = "Single molecules of alkaline phosphatase were assayed using capillary electrophoresis laser-induced fluorescence detection. Multiple incubations of individual molecules were performed. Varying the temperature in multiple incubation assay allowed for the determination of the activation energy of catalysis at the single molecule level. Molecules are heterogeneous with respect to both activity and activation energy of catalysis. Partial thermal denaturation of alkaline phosphatase results from the total denaturation of a fraction of the molecules with surviving molecules unaffected rather than a partial decrease in the activity of all the molecules.",

author = "Craig, {Douglas B.} and Arriaga, {Edgar A.} and Wong, {Jerome C.Y.} and Hui Lu and Dovichi, {Norman J.}",

year = "1997",

month = dec,

day = "1",

doi = "10.1016/S1080-8914(97)80015-4",

language = "English (US)",

volume = "8",

pages = "121--131",

journal = "Techniques in Protein Chemistry",

issn = "1080-8914",

publisher = "Academic Press Inc.",

number = "C",

}

TY - JOUR

T1 - Single alkaline phosphatase molecule assay by capillary electrophoresis laser-induced fluorescence detection

AU - Craig, Douglas B.

AU - Arriaga, Edgar A.

AU - Wong, Jerome C.Y.

AU - Lu, Hui

AU - Dovichi, Norman J.

PY - 1997/12/1

Y1 - 1997/12/1

N2 - Single molecules of alkaline phosphatase were assayed using capillary electrophoresis laser-induced fluorescence detection. Multiple incubations of individual molecules were performed. Varying the temperature in multiple incubation assay allowed for the determination of the activation energy of catalysis at the single molecule level. Molecules are heterogeneous with respect to both activity and activation energy of catalysis. Partial thermal denaturation of alkaline phosphatase results from the total denaturation of a fraction of the molecules with surviving molecules unaffected rather than a partial decrease in the activity of all the molecules.

AB - Single molecules of alkaline phosphatase were assayed using capillary electrophoresis laser-induced fluorescence detection. Multiple incubations of individual molecules were performed. Varying the temperature in multiple incubation assay allowed for the determination of the activation energy of catalysis at the single molecule level. Molecules are heterogeneous with respect to both activity and activation energy of catalysis. Partial thermal denaturation of alkaline phosphatase results from the total denaturation of a fraction of the molecules with surviving molecules unaffected rather than a partial decrease in the activity of all the molecules.

UR - http://www.scopus.com/inward/record.url?scp=77957034615&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77957034615&partnerID=8YFLogxK

U2 - 10.1016/S1080-8914(97)80015-4

DO - 10.1016/S1080-8914(97)80015-4

M3 - Article

AN - SCOPUS:77957034615

VL - 8

SP - 121

EP - 131

JO - Techniques in Protein Chemistry

JF - Techniques in Protein Chemistry

SN - 1080-8914

IS - C

ER -