Journals / Etlik Veteriner Mikrobiyoloji Dergisi / 2007 / Cilt: 18 - Sayı: 1-2

Antifreeze Proteins

Antifriz proteinler

Pages
27–32
Publication Date
2007-12-01
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Nowadays antifreeze proteins are common used in foods, medical and industrial area.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Antifreeze proteins first found in the Notothenioid in Antartic ocean.
📊
Key Findings & Data:Antifreeze proteins family has 5 type of protein, plant and insect form.
💡
Conclusion & Impact:Nowadays antifreeze proteins are common used in foods, medical and industrial area.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Etlik veterinerlik Mikrobiyoloji Dergisi · Antifriz · Protein

Abstract

Antifreeze proteins first found in the Notothenioid in Antartic ocean. The protein consist of a repeated glycopeptide, Ala-Ala-Thr-galactosyl-N-acetyl galactosamine. These glycopeptides made bond with hydroxyl (-OH) and carbonyl (=C=O) groups to the ice crystal to prevent freezing. While ice crystal was entering the skin antifreeze proteins bind to ice crystal, by this way crystal growth can be stopped. Evolution of antifreeze glycoprotein gene from a trypsinogen gene and origin from skin or liver. Antifreeze proteins family has 5 type of protein, plant and insect form. Nowadays antifreeze proteins are common used in foods, medical and industrial area.

Özet

İlk kez Antartik sularda yaşayan Notothenioid’lerde varlığı gösterilen Antifriz proteinler (AFGP ve AFP) her biri üç amino asitlik bir peptid zincirinin üçüncü amino asidine kovalan bağlarla bağlanmış bir disakkarit molekülünden oluşan birimlerin (alanin-alanin-threonin-galaktozil-N-asetilgalaktozamin)n tekrarlanması ile meydana gelen bir glikopeptid yapıdadır. Bu glikopeptidler balığın derisinden vücuda giren ufacık buz kristallerine hidroksil grupları (-OH), diğer polar grupları ve amino asit zincirlerindeki karbonil (=C=O) grupları ile tutunup, kristallerin büyümesini önleyerek canlıyı donmaya karşı korumaktadır. Antifriz proteinlerin tripsinojen genin birtakım çoğalmaları sonucunda oluştuğu ve karaciğer ve deri kaynaklı olabileceği, antifriz protein ailesinin bitki ve böcek tipine ek olarak 5 tip proteini kapsadığı saptanmıştır. Günümüzde bu proteinler tıp, gıda ve endüstri alanlarında etkin biçimde kullanılmaktadır.

🔖

Cite This Article

BEKTAŞ, G. I., ALTINTAŞ, A. (2007). Antifreeze Proteins. Etlik Veteriner Mikrobiyoloji Dergisi, Cilt: 18 - Sayı: 1-2, 27–32. https://ajindex.com/articles/406407

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (16)

  1. Crevel R.W.R, Fedyk J.K, Spurgeon M.J. (2002). Antifreeze proteins: characteristics, occurrence and human exposure (Review). Food and Chemical Toxicology 20, 899-903.
  2. Eastman J.T, Devries A.L. (1986),
  3. Olağan Dışı Yaşam-lar TÜBİTAK, Mart 1999.
  4. Sıdell B.D. (2000)
  5. School of Marine Sciences, University of Maine, Orono ME Gravitational and Space Biology Bulletin 13(2). De Vries A.L., Komatsu S.K., Feeney R.E. (1970). Chemical and physical properties of freezing point-depressing glycoproteins from Antarctic fishes. J Biol Chem. 245:11, 2901-8.
  6. Chen L, De Vries A.L. (1997) Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc. Natl. Acad. Sci. USA Vol. 94, pp. 3811-3816, April 1997,Evolution. Fletcher G.L., Hew C.L., Davies P.L. (2001). Antifreeze Proteins of Teleost Fishes. Annu. Rev. Physiol. 63, 359–90.
  7. Fletcher G.L, Goddard S.V, Wu Y. (1999). Antifreeze proteins and their genes: From basic research to business opportunity. American Chemical Society, Chemtech 30(6),17-28.
  8. Duman J., Devrıes A.L. (1976). Isolation, characterization and physical properties of protein antifreezes from the Winter Flounder Pseudopleunectus Americanus. Comp. Biochem. Physiol. B54, 375–380.
  9. Scotter A.J. (2006). The basis for hyperactivity of antifreeze proteins (Review). Cryobiology doi: 10.1016/j.cryobiol.2006.06.06. Sıcheri F.,.Yang D.S, Nature 3755:427-431, 1995.
  10. Ng N., Hew C. (1992). Structure of antifreeze polypeptide from sea raven: Disulfide bonds and similarity to lectin-binding proteins. J. Biol. Chem. 267 (23): 16069-16075.
  11. Deng G., Andrews D.W., Laursen R.A. (1997). Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis. FEBS Lett. 402:1, 17-20.
  12. Graham L. (1997). Hyperactive antifreeze protein from beetles. Nature 388, 727-728.
  13. Duman J.G. (2001). Antifreeze and Ice Nucleator Proteins in Terrestrial Arthropods. Annu. Rev. Physiol. 63, 327–57.
  14. Graham L., Davies P. (2005) Biophysical Journal Vol:88 (953-958). Kuiper et al, (2001). A Theoretical Model of a Plant Antifreeze Protein from Lolium perenne, Biophysical Journal, Vol: 81, Sayı 6. Grıffıth M., Yaısh M. (2004). Antifreeze proteins in overwintering plants: a tale of two activities. Trends in Plant Science 9:8, 399-405.
  15. Grıffıth M. (1992). Antifreeze Protein Produced Endogenously in Winter Rye Leaves. Plant Physiology 100:2, 593-596.
  16. Clarke C.J., Buckley S.L., Lindner N. (2002) Cryo Letters. Mar-Apr; 23(2):89-92.