Lactoferrin contains structural motifs of ribonuclease

Devi, A. Sharada ; Das, M. R. ; Pandit, M. W. (1994) Lactoferrin contains structural motifs of ribonuclease Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1205 (2). pp. 275-281. ISSN 0167-4838

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A high molecular weight ribonuclease isolated from human milk (hmRNAase) shares identical immunological, physical, structural features and considerable sequence homology with human lactoferrin; and it has been demonstrated to be an isoform of lactoferrin. We have analyzed the sequence data of lactoferrin looking for the existence of specific features corresponding to the consensus sequence of pyrimidine-specific ribonucleases. The analysis was done by comparing sequence features with respect to elements which are, in principle, responsible for RNAase activity. This revealed the existence of a ribonuclease-signature pattern in lactoferrin. Further analysis of x-ray data together with molecular modeling studies have revealed close similarities between the spatial geometry of the constituent groups of the active site of pyrimidine-specific ribonucleases and the corresponding groups comprising the potential active site of lactoferrin. Our results provide the strong structural basis for the existence of ribonuclease activity in lactoferrin.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Pyrimidine-specific Ribonucleases; Homology; Lactoferrin; Active Site
ID Code:8539
Deposited On:27 Oct 2010 06:19
Last Modified:30 May 2011 09:20

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