Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Laminin is structurally conserved in the sea urchin basal lamina

McCarthy, R. A., Beck, Konrad and Burger, M. M. 1987. Laminin is structurally conserved in the sea urchin basal lamina. Embo Journal 6 (6) , pp. 1587-1593.

Full text not available from this repository.


The extracellular matrix is involved in the regulation of differentiation and morphogenesis. Here we report the identification of a sea urchin embryonic extracellular matrix protein by means of a monoclonal antibody BL1 (Mab BL1) and the isolation of the protein from basal lamina preparations. In paraffin sections of fixed embryos, the antibody can be detected on the basal surfaces of cells after the blastula stage. Immunoprecipitation from embryo lysates and salt extracts of metabolically labeled basal lamina preparations demonstrates that the basal lamina antigen is a large mol. wt protein of approximate mol. wt 10 which consists of disulfide-linked subunits of mol. wts 480 000 and 260 000. Electron microscopic images show that the Mab BL1 basal lamina antigen is structurally related to the vertebrate extracellular matrix protein laminin.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Publisher: Nature Publishing Group
ISSN: 0261-4189
Last Modified: 04 Jun 2017 03:04

Citation Data

Cited 50 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item