Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 565

The DOI matches its Crossref record.

Transphosphatidylation by Phospholipase D

Open access
Yang, S.F., Freer, Sofia, Benson, A.A.·1967·Journal of Biological Chemistry

Abstract

Abstract Transphosphatidylase activity was recognized in several plant tissues as well as in extracts. It was attributed to phospholipase D. This enzyme was purified 110-fold from Savoy cabbage. The ratio of its hydrolase to its transphosphatidylase activity remained constant throughout the purification. Additional evidence supports the conclusion that both reactions are catalyzed by the same enzyme. Phosphatidylations of ethanol, ethanolamine, and glycerol were readily achieved by incubating phosphatidylcholine and the enzyme in the presence of one of these acceptors. Concentrations of the acceptors required for equality between rates of hydrolysis and transphosphatidylation were 0.7, 0.3, and 1.1%, respectively, for ethanol, ethanolamine, and glycerol. The glycerol configuration in the phosphatidylglycerol thus produced was dl-; phosphatidylation in this case was not stereospecific. Phospholipase D catalyzed exchange between choline and phosphatidylcholine. Its activity was completely inhibited in 10-4 m p-chloromercuribenzoate. The results implicate formation of a phosphothioester linkage in the phosphatidylenzyme complex. The transphosphatidylase function of phospholipase D offers a useful route for synthesis of a variety of phosphatidyl esters.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)96298-8

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cited by

See all 565

Metadata

Authors
Yang, S. F., Freer, S., & Benson, A. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1967-02
Volume
242
Issue
3
Pages
477-484
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1518259698
Cited by
565
References
0
FWCI
4.12
Type
journal article
Language
en
Open access
hybrid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Transphosphatidylation by Phospholipase D. https://app.cochat.ai/papers/10.1016/s0021-9258(18)96298-8
The paper
Yang, S. F., Freer, S., & Benson, A. A. (1967). Transphosphatidylation by Phospholipase D. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)96298-8

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.