SavedAdd your journal

Journals / İbn-i Sina Tıp Dergisi / 2002 / Cilt: 7 - Sayı: 2

Electrophoretic analysis of erythrocyte membrane proteins precipitated by ammonium sulfate

Amonyum sülfatla çöktürülmüş eritrosit membran proteinlerinin elektroforetik analizi

Vanizor Birgül KURAL
Eşref Edip KEHA
REZZAN ALİYAZICIOĞLU
Pages
84–89
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)

As a result, it was concluded that the protein bands may be more visible and new bands may be observed by the electrophoresis of erythrocyte membrane proteins precipitated ammonium sulfate.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:In the present study, erythrocyte membrane proteins were precipitated by various ammonium sulfate saturation and then their electrophoretic mobilities were analyzed by sodium dodecyl sulfate polyacrilamid gel electrophoresis.
📊
Key Findings & Data:So, when erythrocyte membrane proteins obtained from 30 normal subjects were treated with ammonium sulfate in saturation of 10 %, 20 %, 30 %, 40 % and 50 %, it was observed that almost all protein bands were seen in 10 % saturation of ammonium sulfate while the most exactly seen bands were spectrin dimers in 30 %, 40 % and 50 % saturation.
💡
Conclusion & Impact:As a result, it was concluded that the protein bands may be more visible and new bands may be observed by the electrophoresis of erythrocyte membrane proteins precipitated ammonium sulfate.
🔬Design:Research Article
📍Scope:30 samples
⚙️Variables:Elektroforez · poliakrilamid jel · Amonyum sülfat

Abstract

In the present study, erythrocyte membrane proteins were precipitated by various ammonium sulfate saturation and then their electrophoretic mobilities were analyzed by sodium dodecyl sulfate polyacrilamid gel electrophoresis. So, when erythrocyte membrane proteins obtained from 30 normal subjects were treated with ammonium sulfate in saturation of 10 %, 20 %, 30 %, 40 % and 50 %, it was observed that almost all protein bands were seen in 10 % saturation of ammonium sulfate while the most exactly seen bands were spectrin dimers in 30 %, 40 % and 50 % saturation. Without ammonium sulfate precipitation, protein 4.2 was seen as a unique band but in 10 % saturation, two bands were observed, for 28 of 30 samples, in protein 4.2 region. As a result, it was concluded that the protein bands may be more visible and new bands may be observed by the electrophoresis of erythrocyte membrane proteins precipitated ammonium sulfate.

Özet

Bu çalışmada, eritrosit membran proteinleri çeşitli amonyum sülfat doygunluklarında çöktürülerek, elektroforetik hareketlilikleri, sodyum dodesil sülfat poliakrilamid jel elektroforezi ile izlendi. Bu amaçla 30 normal şahıstan elde edilen eritrosit membran proteinleri, % 10, % 20, % 30, % 40, % 50'lik amonyum sülfat doygunluklarına muamele edildiklerinde %10'luk amonyum sülfat doygunluğunda hemen hemen tüm bantların gözlenebildiği, % 30, % 40 ve % 50'lik doygunluklarda ise en iyi gözlenebilen bantların spektrin dimerleri olduğu tespit edildi. Amonyum sülfatla çöktürme uygulanmadığında, bant 4.2 tek halinde iken, %10'luk amonyum sülfat doygunluğunda, bu bölgede 30 nümunenin 28'inde çift bant görüldü. Sonuç olarak, amonyum sülfat ile çöktürülmüş eritrosit membran proteinlerinin elektroforezinde protein bantlarının daha belirgin olabileceği ve yeni bantlarında gözlenebileceği kanaatına varıldı.

🔖

Cite This Article

KURAL, V. B., KEHA, E. E., ALİYAZICIOĞLU, R. (2002). Electrophoretic analysis of erythrocyte membrane proteins precipitated by ammonium sulfate. İbn-i Sina Tıp Dergisi, Cilt: 7 - Sayı: 2, 84–89. https://ajindex.com/articles/284920

References (12)

  1. Lux SE, Backer P S: Disorders of the cell membrane skeleton. In Goldstein JL and Brown MS, eds., The metabolic basis of whereted disease, Me Graw Hill Book Co., pp. 2367-98, 1983
  2. Fairbanks G, Steck TL, Wallach DFH: Electrophoretic analysis of the major polipeplides of the human erythrocyte membrane. Biochemistry, 10(13): 2606- 2661, 1977
  3. Siegel DL, Branton D: Partial purification and characterization of an actin-bunding protein, band 4.9, from human erythrocvies. J Cell Biol, 100:775-785, 1985. ' 4. Mathews CK, Holde KEV: Biochemistry. The Benjamin/Cumming Publishing Compony, Rech>ood City, pp. 308-317, 1990
  4. Retting MP, Orendorff CJ, Campanella E, Low PS: Effect of pH on the slef- association of erythrocyte band 3 in situ. Biochim Biophys Acta, 1515:72-81, 2001
  5. Lux S, Shohet SB: The erythrocyte membrane skeleton: Biochemistry. Hospital Practice, Oct: 77-83, 1984
  6. Fujinaga J, Tang XB, Casey JR: Topology of the Membrane Domain of Human Erythrocyte Ani on Exchange Protein, AE1. J ' Biol ' Chem, Vol. 2 74(10):6626-6633, 1999
  7. Malik S, Sami M, Watts A: A role for band 4.2 in human erythrocyte band 3 mediated anion transport. Biochemistry, 32:10078- 10084, 1993
  8. Moore RB, Shriver SK: Protein 7.2b of human erythrocyte membranes binds to calpromotin. Biochem Biophys Res Commun, 232(2):294-297, 1997. ' 10. Home W C, Mi etti nen H, Marchesi V T: Erythrocyte membrane skeleton phösphoproteins identification of two unrelated phösphoproteins in band 4.9. Biochim Acta, 944(2): 135-143, 1988. ll.Hamaguchi H, Cleve H /Solubilization of human erythrocyte membrane glycoproteins and separation of the MN glycoprotein from a glycoprotein with I, S and A activity. Biochem Biophys Acta, 278:271-280, 1972. U.Robyt JF, White BJ: Biochemical techniques, theory and practice. Waveland Press, Inc., Waveland, 1987, pp 129-144
  9. Lowry O H, Rosenbrough N L, Farr A L, Rondel R L: Protein measurement with folin phenol reagent. J Biol Chem, 1993:265-275, 1951
  10. Humes BD: One dimensional polyacrylamid gel electrophoresis. In flames BD and Rickwood D, eds., Gel electrophoresis of protein. A practical approach. Second Ed, Oxford University Press, New York, 1990, pp. 1-59. lS.Shohet SB, Lux S: The erythrocyte membrane skeleton: Pathophysiology. Hospital Practice, Nov:89-95, 1984
  11. Sleek TL: The organization of proteins in the human red blood cell membrane. J Cell Biol, 62:1-19, 1974
  12. Cherry L, Men hart N, Fung LW: Interactions of the alpha-spectr