Abstract:
:We describe here the presence of ubiquitin and its conjugation system in the rat retina. Retinal homogenates and supernatants conjugate [125I]human ubiquitin with either endogenous or exogenous proteins. The conjugating activity is relatively stable over time, requires ATP, and has a pH optimum of approximately 8. The most prominent [125I]ubiquitin conjugates formed are larger than 130 kDa. Several other minor conjugates are also formed between the molecular weights 17 and 75 kDa. The endogenous levels of free and conjugated forms of ubiquitin have been determined in the rat retina. More than 50% of retinal ubiquitin is covalently bound to target proteins. In addition, activities responsible for the ATP-dependent degradation and disassembly of both endogenous and exogenous ubiquitin conjugates have been detected in vitro. These results provide evidence that the retina contains active and stable ubiquitin-conjugating enzymes that recognize retinal proteins and have ATP-dependent proteolytic activity.
journal_name
J Neurosci Resjournal_title
Journal of neuroscience researchauthors
Naash M,Izbicka E,Anderson REdoi
10.1002/jnr.490300220subject
Has Abstractpub_date
1991-10-01 00:00:00pages
433-41issue
2eissn
0360-4012issn
1097-4547journal_volume
30pub_type
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