Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expression, purification, and enzymatic properties of recombinant human cytochrome P450c27 (CYP27).

Archives of biochemistry and biophysics - 1 Jul 1997

Pikuleva I A, Björkhem I, Waterman M R

Abstract excerpt

A large number of microsomal P450s have been expressed in Escherichia coli in quantities sufficient for structure/function analysis. However, only one mitochondrial P450 has been successfully overexpressed, that being cholesterol side chain cleavage cytochrome P450 (P450scc). We report here overexpression, purification, and characterization of a second mitochondrial P450, human sterol C-27 hydroxylase (P450c27)....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Cloning, Molecular
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Mutation

Share to Rabbits

Share to Recombinant Proteins

Source

Identifiers

PMID: 9210654
DOI: 10.1006/abbi.1997.0142

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression, purification, and enzymatic properties of recombinant human cytochrome P450c27 (CYP27).PMID 9210654Read ↗

Heterologous expression, purification, and properties of human cytochrome P450 27C1.Semantic proximity Read ↗

A universal approach to the expression of human and rabbit cytochrome P450s of the 2C subfamily in Escherichia coli.Semantic proximity Read ↗

Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties.Semantic proximity Read ↗

Lack of mutations in CYP2D6 and CYP27 in patients with apparent deficiency of vitamin D 25-hydroxylase.Semantic proximity Read ↗

Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1.Semantic proximity Read ↗

Cloning of Human 25-Hydroxyvitamin D-1 -Hydroxylase and Mutations Causing Vitamin D-Dependent Rickets Type 1Semantic proximity Read ↗

Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages.Semantic proximity Read ↗

Rat cytochrome P450C24 (CYP24A1) and the role of F249 in substrate binding and catalytic activity.Semantic proximity Read ↗

Characterization of the consequence of a novel Glu-380 to Asp mutation by expression of functional P450c21 in Escherichia coli.Semantic proximity Read ↗

Functional analysis of mutant P450(C21) genes in COS cell expression system.Semantic proximity Read ↗

Expression of modified human cytochrome P450 1A1 in Escherichia coli: effects of 5' substitution, stabilization, purification, spectral characterization, and catalytic properties.Semantic proximity Read ↗

Substitution at residue 473 confers progesterone 21-hydroxylase activity to cytochrome P450 2C2.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.