Isolation and characterization of uteroglobin from the lung of the hare (Lepus capensis).

Abstract:

:Uteroglobin has been purified from hare lung by gel filtration and chromatography on carboxymethyl-cellulose. Hare uteroglobin appears homogeneous by electrophoresis under both denaturing and nondenaturing conditions. Its chemical and immunological properties as well as its ability to bind progesterone are compared to those of rabbit uteroglobin. The two proteins have the same N-terminal residue (glycine) and both lack tryptophan but differ in amino acid composition. Sodium dodecyl sulfate-gel electrophoresis shows that hare uteroglobin is composed of two subunits of identical Mr (about 7000) held together by disulfide bridges. The amino acid composition indicates a subunit composed of 65-67 residues, which is compatible with the apparent Mr observed. Thus, hare uteroglobin appears to be slightly smaller than the rabbit protein. Hare uteroglobin partially reacts with anti-rabbit uteroglobin in a radioimmunoassay and also binds progesterone, although this binding is relatively unaffected by dithiothreitol. The synthesis of hare uteroglobin in the uterus appears to be rather insensitive to ovarian steroid hormones.

journal_name

Arch Biochem Biophys

authors

Soledad López de Haro M,Nieto A

doi

10.1016/0003-9861(83)90323-5

subject

Has Abstract

pub_date

1983-10-15 00:00:00

pages

539-47

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(83)90323-5

journal_volume

226

pub_type

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