TY  - JOUR
T1  - Beta-Keratins of Reptilian Scales Share a Central Amino Acid Sequence Termed Core-Box
AU - , Lorenzo Alibardi AU - , Mattia Toni 
JO  - Research Journal of Biological Sciences
VL  - 2
IS  - 3
SP  - 329
EP  - 339
PY  - 2007
DA  - 2001/08/19
SN  - 1815-8846
DO  - rjbsci.2007.329.339
UR  - https://makhillpublications.co/view-article.php?doi=rjbsci.2007.329.339
KW  - Reptiles
KW  -epidermis
KW  -beta keratins
KW  -electrophoresis
KW  -immunoblotting
KW  -immunocytochemistry
AB  - Beta-keratins determine most of mechanical resistance of reptilian scales. The amino acid sequence of these proteins is not known for most reptiles. An antibody directed against a known  20-amino acid sequence (core-box) of avian beta-keratins has been utilized to detect whether this  epitope is also present in reptilian beta-keratins. The epidermis of most tested species (lepidosaurians, tuatara, chelonians andcrocodilians) shows immunoreactivity in the beta-layer.  In immunoblots, specific immunolabeled bands are seen, mainly within 10-25 kDa (beta-keratin  range). Bidimensional gel electrophoresis shows that most beta-keratins are basic proteins and  contain the epitope for the presence of a core-box. The core-box is conserved among reptile and  bird beta-keratins and seems linked to their structural properties in the formation of hard keratin  packets. The only exception is represented by the soft shelled-turtle (Tryonix spiniferus). The  latter species probably lacks the core-box in its beta-keratin and therefore cannot accumulate beta-keratin packets in the corneous layer explaining the softness of its shell. The molecular analysis on some known beta-keratin sequences suggests that the core-box epitope is centrally located in beta-keratins.
ER  -