Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site.

• DOI: 10.1073/pnas.87.1.26
• Publication Date: 2006-05-31T11:18:56Z
• Authors: S O Brennan; T Myles; R J Peach; D Donaldson; P M George
• Keywords: Signal peptidase; Protein precursor; Serum Albumin; Cleavage (geology)

Albumin Redhill is an electrophoretically slow genetic variant of human serum albumin that does not bind 63Ni2+ and has a molecular mass 2.5 kDa higher than normal albumin. Its inability to Ni2+ was explained by the finding additional residue Arg at position -1. This did explain basis variation (since proalbumin contains adjacent residues -1 -2) or increase in apparent mass. Fractionation tryptic digests on concanavalin A-Sepharose followed peptide mapping bound unbound fractions sequence analysis glycopeptides identified mutation 320 Ala----Thr. introduces Asn-Tyr-Thr oligosaccharide attachment centered Asn-318 explains This, however, satisfactorily presence DNA sequencing polymerase chain reaction-amplified genomic encoding prepro indicated -2 Arg----Cys. sequence, Met-Lys-Trp-Val-Thr-Phe-Ile-Ser-Leu-Leu-Phe-Leu-Phe-Ser-Ser-Ala-Tyr- Ser-Arg-Gly-Val-Phe-Cys-Arg (cf.-Tyr-Ser-Arg-Gly-Val-Phe-Arg-Arg- pre-proalbumin). We propose new Phe-Cys-Arg propeptide aberrant signal peptidase cleavage site cleaves lumen endoplasmic reticulum before it reaches Golgi vesicles, diarginyl-specific convertase.