Vitamin D-binding protein (DBP) is a multifunctional, highly expressed, polymorphic serum protein[1][2]. ?Since its identification in 1959, many important functions of Vitamin D binding protein have been discovered. These range from the transport of vitamin D metabolites to possible roles in the immune system and host defense[3]. The molecular weight range, time course of appearance, and effect of dietary strontium all suggested that the newly appearing protein( band C) might represent the calcium binding protein formed in response to vitamin D. Using chromatographically purified calcium binding protein from rat intestine, it was shown that this protein(band C) most probably is the calcium binding protein. The major contaminating protein in the final purification of rat calcium binding protein has also been identified on gels as the preexisting protein (band A), which is probably the precursor of the calcium binding protein.[4].

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Ref:

[1] N.E. Cooke, J.G. Haddad, Vitamin D binding protein (Gc-globulin), Endocr. Rev., 10 (1989), pp. 294–307

[2] N.E. Cooke, J.G. Haddad, Vitamin D binding protein (Gc-globulin): update 1995, A. Negro-Vilar, D.D. Bikle (Eds.), Endocrine Reviews Monographs: 4. Hormonal Regulation of Bone Mineral Metabolism, The Endocrine Society (1995), pp. 125–128

[3] Peter White,? Nancy Cooke, “The Multifunctional Properties and Characteristics of Vitamin D-binding Protein”,Volume 11, Issue 8, 1 October 2000, Pages 320–327.

[4] H. F. DeLuca?,?D. Drescher, Possible precursor of vitamin D-stimulated calcium binding protein in rats, Biochemistry,?1971,?10?(12), pp 2308–2312 , DOI:?10.1021/bi00788a020, Publication Date: June 1971.

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