TY - JOUR
T1 - Proteins of the gelatinous layer of the trout saccular otolithic membrane
AU - Khan, Khalid M.
AU - Drescher, Dennis G.
N1 - Funding Information:
This work was supportedb y NIH Grant NS 16166t o D.G.D.
PY - 1990/1
Y1 - 1990/1
N2 - Although the otolithic membrane is thought to play an important role in the stimulation of vestibular hair cells, little is known about its chemical composition. We analyzed proteins of the gelatinous layer of this structure from the trout saccule, a probable organ of hearing in fish, by SDS-polyacrylamide gel electrophoresis. A relatively small number of major proteins were detected in homogenates of the 'membrane' layer, with apparent molecular weights ranging from 35 to >300 kDa. Six bands, with molecular weights of 35, 43, 65, 94, 100, and 160 kDa, were particularly prominent. Periodic acid-Schiff (PAS) staining indicated that the 43, 94, 100, and 160 kDa bands were glycoproteins. Lectin binding on nitrocellulose blots confirmed the PAS results, and further suggested that the 35 and 65 kDa bands may be glycoproteins. Incubation of blots with human anti-collagen type II antibodies suggested that the 94 kDa band was a component of collagen type II or a related protein.
AB - Although the otolithic membrane is thought to play an important role in the stimulation of vestibular hair cells, little is known about its chemical composition. We analyzed proteins of the gelatinous layer of this structure from the trout saccule, a probable organ of hearing in fish, by SDS-polyacrylamide gel electrophoresis. A relatively small number of major proteins were detected in homogenates of the 'membrane' layer, with apparent molecular weights ranging from 35 to >300 kDa. Six bands, with molecular weights of 35, 43, 65, 94, 100, and 160 kDa, were particularly prominent. Periodic acid-Schiff (PAS) staining indicated that the 43, 94, 100, and 160 kDa bands were glycoproteins. Lectin binding on nitrocellulose blots confirmed the PAS results, and further suggested that the 35 and 65 kDa bands may be glycoproteins. Incubation of blots with human anti-collagen type II antibodies suggested that the 94 kDa band was a component of collagen type II or a related protein.
KW - Collagen
KW - Electroblotting
KW - Lectin binding
KW - Otolithic membrane
KW - Polyacrylamide gel electrophoresis
KW - Saccule
UR - http://www.scopus.com/inward/record.url?scp=0025021828&partnerID=8YFLogxK
U2 - 10.1016/0378-5955(90)90224-D
DO - 10.1016/0378-5955(90)90224-D
M3 - Article
C2 - 1690197
AN - SCOPUS:0025021828
SN - 0378-5955
VL - 43
SP - 149
EP - 158
JO - Hearing Research
JF - Hearing Research
IS - 2-3
ER -