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A Protein in Normal Nurse Shark Serum which Reacts Specifically with Fructosans

II. Physicochemical Studies^1,2,

From the Departments of Microbiology, Neurology, and Human Genetics and Development, College of Physicians and Surgeons, Columbia University, and the Neurological Institute, Presbyterian Hospital, New York 10032 and the Department of Microbiology, University of Miami, Florida 33155

Abstract

The purified fructosan-specific protein (FSP) from normal nurse shark serum showed several bands in acrylamide gel electrophoresis, pH 9.3. Three purified preparations from three individual sharks appeared to have the same banding pattern but two pools from four shark sera showed a different band distribution. One preparation of FSP appeared as a single symmetrical peak on analytical ultracentrifugation with an s of 10.64; the other showed two bands. The molecular weight calculated from sedimentation velocity, viscosity measurement and partial specific volume is 280,500. The protein contains four subunits linked noncovalently. Amino acid analysis showed large amounts of aspartic acid, glutamic acid, serine, threonine and cystine. No carbohydrate was detected. The circular dichroism spectrum of the purified FSP showed a negative peak at 220 to 222.5 nm. In the near ultraviolet, three positive bands were seen at 289, 280 and 268 nm. When sugars which bind specifically to FSP were added to the protein solution, increased ellipticities were seen between 260 to 285 nm with no change below 240 nm.

Footnotes

¹ Aided by grants from the National Science Foundation (GB-8341 and GB-25686) to Dr. E. A. Kabat and a General Research Support grant of the United States Public Health Service to Columbia University; the Spectropolarimeter was available under Program Project Grant GM-18153 to the Department of Human Genetics and Development from the National Institutes of Health; and United States Public Health Service Research Grant AI-05758 from the National Institute of Allergy and Infectious Disease to the University of Miami (Dr. M. M. Sigel).

² From Part II of a dissertation submitted by V. Harisdangkul in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Faculty of Pure Science, Columbia University, New York.

³ Rockefeller Foundation Fellow, 1967–1971.