@article{0253880db41c4b99868f0fad045a6409,
title = "Saccharomyces cerevisiae α-factor prevents formation of glycoproteins in a cells",
abstract = "α-Factor inhibits incorporation of [14C]glucosamine into water-soluble and into SDS-extractable glycoproteins to about 90%. The incorporation into chitin is not affected and the same is true for [14C]phenylalanine incorporation into protein. The inhibition of glycoprotein synthesis is specific for a cells.",
keywords = "Cell cycle, G1 arrest, Glycoprotein, Yeast, α-Factor",
author = "Peter Orlean and Gabi Seebacher and Widmar Tanner",
note = "Funding Information: [l-{\textquoteleft}4C]Glucosamine-labeISleDdS, -insolublpee lletsw ere obtaineodn fractionatioonf S. cerevisiuXe 2 180-lac ells radiolabelleidn the absencea nd presencoef a-factor usingt hem ethodin table1 ,a nd successiveelxyt racteadt 98°Cw ith 1.0M HCI and 1.0 M NaOH, as detailedin section2 . Total solublea ndi nsoluble(= mainlyc hitin) radioactivitwy as determined to water-soluble and into SDS-extractable glycoproteinsw asi nhibitedb y up to 90%) whereas the effect on non-extractableg lycoproteinsp lus chitin was small. When the non-solubilizable polymers were treatedw ith hot acid and base to removea ll materialb ut chitin [7] therew as no dif-ferencei n the radioactivityo f the residualc hitin or at beste vena slight increase( table2 ). That the remaining insoluble material indeed is chitin was supported by the observationt hat 80% of this radioactivity was degraded by chitinase (not shown). The resultso f table 1 also showt hat CY-factor does not affect the incorporation of [14C]phenylalaninein to any of the various fractions.",
year = "1983",
month = jul,
day = "25",
doi = "10.1016/0014-5793(83)80588-2",
language = "English (US)",
volume = "158",
pages = "247--251",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",
}