Melcalin® Pralbumina

Melcalin Pralbumina is a food supplement containing Proteins and Minerals. Proteins contribute to the growth and maintenance of muscle mass while minerals help electrolyte balance and the reduction of tiredness and fatigue.

Melcalin Pralbumina is gluten and lactose free.

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    Description

    PRALBUMINA is a food supplement based on proteins (egg white) and minerals. The product supplements the albumin properties to those of a very low PRAL (-35).
    Albumin regulates and maintains the osmotic pressure necessary for the proper distribution of body fluids intra and extracellular (ECW-ICW), modulates vascular tone, regulates the acid-base balance, has antioxidant functions and scavenger, acts as a transport of hormones and toxic substances by acting as
    chelating of metals such as copper, zinc, cadmium, nickel and cobalt. These properties are integrated with those arising from the assumption of buffer elements (very negative value of PRAL-Potential Renal Acid Load) which are of considerable benefit for the maintenance of muscle mass (FFM Skeletal muscle, TBprotein) and skeletal (bone) and for the improvement of various problems in the cardio-vascular system load.

    Melcalin® Pralbumina

    Fields of application

    • Adjuvant in the recovery of muscle mass,
    • Regulation of the correct distribution of intra and extracellular fluids: osmotic balance,
    • Regulation of tissue acid-base balance,
    • Antioxidant action,
    • Binding and transport of toxic substances / catabolites

    Bibliography

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    • Evans TW. Review article: albumin as a drug–biological effects of albumin unrelated to oncotic pressure. Aliment Pharmacol Ther. 2002 Dec;16 Suppl 5:6-11.
    • Silvia Martini, Claudia Bonechi, Mario Casolaro, Gianfranco Corbini, Claudio Rossi, –protein recognition processes investigated by NMR relaxation data: A study on corticosteroid – albumin interactions. Biochemical Pharmacology Volume 71, Issue 6, 14 March 2006, Pages 858-864
    • Marcel J.E. Fischer, Octaaf J.M. Bos, RenéF. van der Linden, Jaap Wilting, Lambert. H.M. Janssen Steroid binding to human serum albumin and fragments thereof: Role of protein conformation and fatty acid content. Biochemical Pharmacology Volume 45, Issue 12, 22 June 1993, Pages 2411-2416
    • Michael E Baker. Albumin ‘s role in steroid hormone action and the origins of vertebrates: is albumin an essential protein?. Flebs Letter Volume 439, Issues 1-2, 13 November 1998, Pages 9-12
    • Wojciech Bala, , John Christodouloub, Peter J. Sadlerc, Alan Tucker. Multi-metal binding site of serum albumin. Journal of Inorganic Biochemistry Volume 70, Issue 1, April 1998, Pages 33-39
    • Sakda T. Trisak, Prayong Doumgdee, Bernd M. Rode. Binding of zinc and cadmium to human serum albumin. International Journal of Biochemistry Volume 22, Issue 9, 1990, Pages 977-981
    • P. Bourassa, I. Hasni, H.A. Tajmir-Riahi. Folic acid complexes with human and bovine serum albumins. Food Chemistry Volume 129, Issue 3, 1 December 2011, Pages 1148-1155
    • Bernhard Kreymann , , Markus Seige, Ursula Schweigart, Klaus-Friedrich Kopp, Meinhard Classen. Albumin dialysis: effective removal of copper in a patient with fulminant Wilson disease and successful bridging to liver transplantation: a new possibility for the elimination of protein-bound toxins. Journal of Hepatology Volume 31,
    • Issue 6, December 1999, Pages 1080-1085 Soko?owska M, Wszelaka-Rylik M, Pozna?ski J, Bal W. Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin. J Inorg Biochem. 2009 Jul;103(7):1005-13. Epub 2009 May 3.
    • David Bar-Or, Leonard T. Rael, Raphael Bar-Or, Denetta S. Slone, Charles W. Mains, Nagaraja K.R. Rao, C. Gerald Curtis. The cobalt–albumin binding assay: Insights into its mode of action. Clinica Chimica Acta Volume 387, Issues 1-2, January 2008, Pages 120-127
    • Bruttomesso D, Iori E, Kiwanuka E, Zanetti M, Pianta A, Vettore M, Tiengo A, Tessari P. Insulin infusion normalizes fasting and post-prandial albumin and fibrinogen synthesis in Type 1 diabetes mellitus. Diabet Med. 2001 Nov;18(11):915-20.
    • Pierpaolo De Feo,t Margaret Gan Gaisano and Morey W. Haymond. Differential Effects of Insulin Deficiency on Albumin and Fibrinogen Synthesis in Humans.
    • J.Clin.Invest. Vol 88, Sept.1991, 833-840
    • Han J. Moshage, Hans J.W. de Haard, Hans M.G. Princen, Sing Hiem Yap. The influence of glucocorticoid on albumin synthesis and its messenger RNA in rat in vivo and in hepatocyte suspension culture. Biochimica et Biophysica Acta (BBA) – Gene Structure and Expression Volume 824, Issue 1, 29 January 1985, Pages 27-33
    • Chih-Dou Chou, Huey-Wen Yien, Der-Min Wu, Cheng-Deng Kuo, Albumin Administration in Patients with Severe Sepsis Due to Secondary Peritonitis. Journal of the Chinese Medical Association Volume 72, Issue 5, May 2009.
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    • Philip Goldwasser, Joseph Feldman. Association of serum albumin and mortality risk. Journal of Clinical Epidemiology Volume 50, Issue 6, June 1997, Pages 693-703
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    • Murakami K, Sasaki S, Takahashi Y, Uenishi K. Association between dietary acid-base load and cardiometabolic risk factors in young Japanese women. Br J Nutr. 2008 Sep;100(3):642-51. Epub 2008 Feb 18.
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    Melcalin® Pralbumina

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