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Acid phosphatases bind to the main high density lipoprotein apolipoprotein A‐I
Author(s) -
Vihko P.,
Wahlberg L.,
Ehnholm C.,
Lukka M.,
Vihko R.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80707-4
Subject(s) - chemistry , apolipoprotein b , acid phosphatase , biochemistry , phosphatase , prostatic acid phosphatase , enzyme , lipoprotein , affinity chromatography , elution , dusp6 , chromatography , apolipoprotein e , cholesterol , protein phosphatase 2 , medicine , disease
The serum protein binding secretory prostatic acid phosphatase (PAP) and lysosomal placental acid phosphatase (LAP) was purified using affinity chromatography on gels containing immobilized acid phosphatases. The protein, which could be eluted from these enzyme affinity gels only with 0.05 HCl (pH 2.0), was shown to be apolipoprotein A‐I (apo A‐I), the main structural protein of high density lipoprotein (HDL).