title: Purification, spectroscopic characterization and o-diphenoloxidase activity of hemocyanin from a freshwater gastropod: Pila globosa.
abstract: Hemocyanins are multi-subunit oxygen carrier proteins, found in select species of arthropoda and mollusca. Here, we have purified native hemocyanin from Pila globosa, a freshwater gastropod, verified using mass spectrometry and determined its molecular weight, secondary structure and the spectral properties, using Ultraviolet/visible, Fourier transform infra-red and Circular dichroism spectroscopy. Our results reveal the oligomeric and glycosylated nature of the protein, comprising of 400 kDa subunits, organized predominantly into a thermo-stable, alpha-helical conformation. Further, biochemical assays confirm catecholoxidase-like activity in hemocyanin, which has been used to develop a first-generation optical sensor, for the detection of phenols.
authors: Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Vidyagiri, Prasanthi Nilayam, Puttaparthy, Anantapur, 515134, Andhra Pradesh, India.
authors: K N
authors: KN
authors: Naresh
authors: S
authors: S
authors: Krupanidhi
authors: S S
authors: SS
authors: Rajan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004156:Catechol Oxidase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D002942:Circular Dichroism; D004795:Enzyme Stability; D005618:Fresh Water; D006031:Glycosylation; D006433:Hemocyanins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D012908:Snails / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D006433:Hemocyanins; D004156:Catechol Oxidase
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