The apparent molecular size of native α‐crystallin B in non‐lenticular tissues

FEBS Letters

Mann, Eric¹  Chiesa, Raúl²  Spector, Abraham²  McDermott, Martin J.² 

[1] Department of Biochemistry, Albert Einstein College of Medicine, New York, NY, USA;Biochemistry and Molecular Biology Laboratory, Department of Ophthalmology, College of Physicians & Surgeons of Columbia University, New York, NY, USA

关键词: Lens protein;    α-Crystallin;    Protein structure;    Protein aggregation;   

DOI  :  10.1016/0014-5793(90)81013-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The apparent molecular size of the native α-crystallin B in cytosol preparations from rat heart, brain and retina was determined by gel permeation chromatography, detecting the protein by immunochemical assay (ELISA), using an α-crystallin specific antiserum. Native α-crystallin from cytosol preparations of rat lens cortex was used as a reference. α-Crystallin B present in all three cytosol preparations from non-lenticular tissues eluted in a single symmetrical peak, with the same elution volume as α-crystallin from lens cortex cytosol preparations, corresponding to an apparent average molecular size of 0.8 × 10⁶ Da. No other species could be detected. The results indicate that the α-crystallin aggregates characterized by an apparent average molecular mass of 0.8 × 10⁶ Da, and considered to be the native, physiological form of the protein in the lens, are indeed not specific to lens tissue. Furthermore, the size of these α-crystallin aggregates is independent of their polypeptide composition. Aggregates found in the lens, composed of αA and αB polypeptides and their respective phosphorylated forms αA_p and αB_p, are similar in size to those found in heart, brain and retina, containing the αB but not the αA polypeptide.

【 授权许可】

Unknown