Biophysical Studies on the Interaction of Isoquinoline Alkaloids with Serum Albumins
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Biophysical Studies on the Interaction of Isoquinoline Alkaloids with Serum Albumins
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| Creator |
Khan, Asma Yasmeen
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| Subject |
Chemistry
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| Description |
Joseph F. Foster first suggested that the model of albumin was a flexible linkage of semiindependent domains (Foster, 1960). The name albumin derives from the early German term albumen, generally indicating proteins. Albumen, on the other hand, derives from the Latin word albus (white) indicating the white part of the cooked egg surrounding the yolk. The protein component of the egg white makes part of a heterogeneous group of proteins, broadly indicated as albumins, including serum albumin, milk albumin and urinary proteins. More specifically, serum albumin is a member of a family of homologous proteins characterized by distinctive structural features with peculiar ligand binding properties. Members of this family are -fetoprotein (AFP), afamin (AFM; also named -albumin), and vitamin D binding protein (DBP) (Peters, 1996; Fasano et al., 2007). Serum albumin was recognized as the principal component of the blood as early as 1839. It has been a model protein for many years for physiological studies. It is the most abundant soluble protein in the circulatory system comprising of about 52-60% of the total plasma protein content.
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| Date |
2013
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| Type |
Thesis
NonPeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/2072/1/ASMA_YASMEEN_KHAN%2C_Ph.D._Thesis.pdf
Khan, Asma Yasmeen (2013) Biophysical Studies on the Interaction of Isoquinoline Alkaloids with Serum Albumins. PhD thesis, Jadavpur University. |
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| Relation |
http://www.eprints.iicb.res.in/2072/
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