Abstract
A low molecular weight (LMW) protein was isolated from bovine tongue epithelium and an antiserum to this protein elicited in rabbits. The indirect peroxidase-antiperoxidase (PAP) technique was used to localize LMW protein in several tissues from six mammalian species: cow, rat, mouse, squirrel, rabbit, and man. Immunoreactivity was demonstrable in stratified squamous epithelia from skin, tongue, cheek, esophagus, vagina, and palate. Epidermal derivatives, such as hair follicles, sebaceous glands and ducts of certain glands were also positively stained. Cornea exhibited weak immunoreactivity as did rabbit bladder. Other types of epithelia including those seen in kidney, thyroid, intestine, trachea, liver, submandibular gland, pancreas and uterus, were not immunoreactive when tested with antiserum to LMW protein. The antiserum was rendered unreactive after absorption with LMW protein but, when absorbed with a keratin polypeptide, most of the immunoreactivity was preserved. It is concluded that the distribution of the soluble LMW protein is similar to that of the insoluble keratin proteins in stratified squamous epithelia but the former is not demonstrable in many simple epithelia that contain keratins.
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