Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 360

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Purification and properties of a new enzyme, N, N-dimethylarginine dimethylaminohydrolase, from rat kidney

Open access
Ogawa, T, Kimoto, M, Sasaoka, K·1989·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)81786-0
Open this paper in CoChat — free account

Abstract

A new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase which plays a role in the metabolism of NG,NG-dimethyl-L-arginine, has been purified to homogeneity from rat kidney. The enzyme consists of a single polypeptide and its molecular weight is about 33,000. The isoelectric point of the enzyme is at pH 5.2. The enzyme catalyzes the hydrolytic liberation of the dimethylamino moiety of NG,NG-dimethyl-L-arginine and forms L-citrulline and dimethylamine. It is highly specific for NG,NG-dimethyl-L-arginine and NG-monomethyl-L-arginine, and the Km values for these amino acids are 0.18 and 0.36 mM, respectively. The enzyme shows the maximum activity at pH 6.5 and requires no cofactor. The activity is strongly inhibited by SH-blocking reagents (e.g. p-chloromercuribenzoate and HgCl2) and divalent metal ions (e.g. Cd2+, Cu2+, and Zn2+).

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)81786-0

Cites

23 of 23 references verified0 citation errors · 0 not checkable

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

Cites

Show all 23 references

Cited by

See all 360

Metadata

Authors
Ogawa, T., Kimoto, M., & Sasaoka, K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1989-06
Volume
264
Issue
17
Pages
10205-10209
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)81786-0
OpenAlex
W1583601846
Cited by
360
References
23
FWCI
2.08
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: Purification and properties of a new enzyme, N, N-dimethylarginine dimethylaminohydrolase, from rat kidney. https://app.cochat.ai/papers/10.1016/s0021-9258(18)81786-0
The paper
Ogawa, T., Kimoto, M., & Sasaoka, K. (1989). Purification and properties of a new enzyme, N, N-dimethylarginine dimethylaminohydrolase, from rat kidney. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)81786-0

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.