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Is there a specific lysophospholipase in human pancreatic juice?

Duan, Rui-Dong LU and Borgström, Bengt (1993) In Biochimica et Biophysica Acta 1167(3). p.326-330
Abstract
The existence of a specific lysophospholipase in human pancreatic juice was evaluated. The proteins were separated by a series of chromatographic steps including Sephacryl S-200, cholate-Sepharose 4B, Sephadex G-100 and CM-Sephadex G-50. The enzyme activities against 1-palmitoyl lysolecithin (LL) as well as tributyrin (TB) and p-nitrophenyl butyrate (PNPB) were determined in all the fractions of these purification procedures. Enzyme activity against LL was always eluted in parallel with activities against TB and PNPB, and no unique activity against LL could be found. The specific activity against LL was 40-times lower than that against PNPB and 200-times lower than that against TB. It is concluded that there is no unique lysophospholipase... (More)
The existence of a specific lysophospholipase in human pancreatic juice was evaluated. The proteins were separated by a series of chromatographic steps including Sephacryl S-200, cholate-Sepharose 4B, Sephadex G-100 and CM-Sephadex G-50. The enzyme activities against 1-palmitoyl lysolecithin (LL) as well as tributyrin (TB) and p-nitrophenyl butyrate (PNPB) were determined in all the fractions of these purification procedures. Enzyme activity against LL was always eluted in parallel with activities against TB and PNPB, and no unique activity against LL could be found. The specific activity against LL was 40-times lower than that against PNPB and 200-times lower than that against TB. It is concluded that there is no unique lysophospholipase in human pancreatic juice and that the hydrolysis of lysolecithin is most likely performed by carboxyl ester lipase. (Less)
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Contribution to journal
publication status
published
subject
in
Biochimica et Biophysica Acta
volume
1167
issue
3
pages
5 pages
publisher
Elsevier
external identifiers
  • scopus:0027154721
ISSN
0006-3002
DOI
10.1016/0005-2760(93)90236-3
language
English
LU publication?
yes
id
1454023c-8c86-4140-a875-32c2f9b48831
date added to LUP
2019-02-03 09:49:51
date last changed
2024-01-15 13:44:28
@article{1454023c-8c86-4140-a875-32c2f9b48831,
  abstract     = {{The existence of a specific lysophospholipase in human pancreatic juice was evaluated. The proteins were separated by a series of chromatographic steps including Sephacryl S-200, cholate-Sepharose 4B, Sephadex G-100 and CM-Sephadex G-50. The enzyme activities against 1-palmitoyl lysolecithin (LL) as well as tributyrin (TB) and p-nitrophenyl butyrate (PNPB) were determined in all the fractions of these purification procedures. Enzyme activity against LL was always eluted in parallel with activities against TB and PNPB, and no unique activity against LL could be found. The specific activity against LL was 40-times lower than that against PNPB and 200-times lower than that against TB. It is concluded that there is no unique lysophospholipase in human pancreatic juice and that the hydrolysis of lysolecithin is most likely performed by carboxyl ester lipase.}},
  author       = {{Duan, Rui-Dong and Borgström, Bengt}},
  issn         = {{0006-3002}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{326--330}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta}},
  title        = {{Is there a specific lysophospholipase in human pancreatic juice?}},
  url          = {{http://dx.doi.org/10.1016/0005-2760(93)90236-3}},
  doi          = {{10.1016/0005-2760(93)90236-3}},
  volume       = {{1167}},
  year         = {{1993}},
}