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(Investigative Ophthalmology and Visual Science. 1966;5:601-609.)
© 1966 by The Association for Research in Vision and Ophthalmology, Inc.

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Alpha, beta, and gamma crystallins in the ocular lens of rabbits: Preparation and partial characterization

Cole V. Mason 1 and Marvin C. Hines 1

1 John E. Weeks Memorial Laboratory, Departments of Ophthalmology and of Biochemistry, University of Oregon Medical School, Portland, Ore.

Alpha, beta, and gamma crystallins from rabbit eye lens have been prepared by continuousflow paper electrophoresis and gel filtration. These methods yielded well-defined fractions in a highly reproducible manner with essentially quantitative recovery of material. The behavior of each of the crystallins in diethylaminoethyl cellulose has been examined. Sidfhydryl ontents of 2.9, 6.1, and 26.0 moles per 105 Gm. of protein were found for alpha, beta, and gamma crystallin, respectively. These values were altered to 5.9 and 8.5 for alpha and beta crystallin in 8 M urea, but that for gamma crystallin was unchanged. Extinction coefficients, E2801%, of 8.3, 21.5, and 17.6 were found for alpha, beta, and gamma crystallin, respectively. Sedimentation constants of 18.9 S and 2.5 S were calculated for alpha and gamma crystalline, respectively. Glycine was found to be the N-terminal amino acid of gamma crystallin. The presence of free N-terminal amino acids for alpha and beta crystallins could not be demonstrated. For these parameters, the characteristics of the rabbit lens crystallins are similar to those of bovine origin

Note:

This investigation was supported in part by United States Public Health Service Research Grant NB 04770-02, from the National Institute for Neurological Diseases and Blindness, in part by a Fight for Sight Student Fellowship financed by a grant from Burroughs Wellcome and Company (U. S. A.), Inc., to the National Council to Combat Blindness, Inc., New York City, and in part by Public Health Service Training Grant 5 Tl GM 1200-02 BCH. Taken in part from a thesis submitted to the Department of Biochemistry, University of Oregon Medical School, in partial fulfillment of the requirements for the Master of Science degree. All inquiries regarding this paper should be sent to Dr. Hines

Taken in part from a thesis submitted to the Department of Biochemistry, University of Oregon Medical School, in partial fulfillment of the requirements for the Master of Science degree

All inquiries regarding this paper should be sent to Dr. Hines






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Copyright © 1966 by the Association for Research in Vision and Ophthalmology