## Abstract In the stratum granulosum of mammalian epidermis, histidinโrich proteins (filaggrins) determine keratin clumping and matrix formation into terminal keratinocytes of the stratum corneum. The nature of matrix, interkeratin proteins in the epidermis of nonmammalian vertebrates, and in part
Morphological and biophysical identification of fibrous proteins in the amniote epidermis
โ Scribed by Baden, H. P. ;Maderson, P. F. A.
- Publisher
- John Wiley and Sons
- Year
- 1970
- Tongue
- English
- Weight
- 784 KB
- Volume
- 174
- Category
- Article
- ISSN
- 0022-104X
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โฆ Synopsis
Abstract
Epidermal material from a variety of reptilian species, avian and mammalian scales have been examined by standard histological and xโray diffraction techniques. It has been found that morphologic and/or tinctorial properties are not good criteria for the identification of specific fibrous protein types. The distribution of fibrous protein types in reptilian epidermal material is very variable, especially in turtles. Lepidosaurian reptiles (the tuatara, snakes and lizards) are unique in showing an alternating vertical distribution of feather and ฮฑโtype proteins over the entire body surface. The protein distribution in crocodilian scales resembles exactly that found on avian scales. Mammals only possess the ฮฑโtype protein whatever the nature of the epidermal structure of modification.
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## Abstract In amphibian epidermis mucus is thought to constitute the matrix material that links keratin filaments present in cells of the corneous layer. As contrast in mammals, and perhaps in all amniotes, histidineโrich proteins form the matrix material. In order to address the study of matrix m
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