TY - JOUR
T1 - Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes
T2 - Comparison with endoplasmic reticulum and mitochondrial membranes
AU - Fujiki, Yukio
AU - Fowler, Stanley
AU - Shio, Helen
AU - Hubbard, L.
AU - Lazarow, Paul B.
PY - 1982/4/1
Y1 - 1982/4/1
N2 - Membranes were isolated from highly purified peroxisomes, mitochondria, and rough and smooth microsomes of rat liver by the one-step Na2CO3 procedure described in the accompanying paper (1982, J. Cell Biol. 93: 97-102). The polypeptide compositions of these membranes were determined by SDS PAGE and found to be greatly dissimilar. The peroxisomal membrane contains 12% of the peroxisomal protein and consists of three major polypeptides (21,700, 67,700 and 69,700 daltons) as well as some minor polypeptides. The major peroxisomal membrane proteins as well as most of the minor ones are absent from the endoplasmic reticulum (ER). Conversely, most ER proteins are absent from peroxisomes. By electron microscopy, purified peroxisomal membranes are ~6.8 nm thick and have a typical trilaminar appearance. The phospholipid/protein ratio of peroxisomal membranes is ~200 nmol/mg; the principal phospholipids are phosphatidyl choline and phosphatidyl ethanolamine, as in ER and mitochondrial membranes. In contrast to the mitochondria, peroxisomal membranes contain no cardiolipin. All the membranes investigated contain a polypeptide band with a molecular mass of ~15,000 daltons. Whether this represents an exceptional common membrane protein or a coincidence is unknown. The implications of these results for the biogenesis of peroxisomes are discussed.
AB - Membranes were isolated from highly purified peroxisomes, mitochondria, and rough and smooth microsomes of rat liver by the one-step Na2CO3 procedure described in the accompanying paper (1982, J. Cell Biol. 93: 97-102). The polypeptide compositions of these membranes were determined by SDS PAGE and found to be greatly dissimilar. The peroxisomal membrane contains 12% of the peroxisomal protein and consists of three major polypeptides (21,700, 67,700 and 69,700 daltons) as well as some minor polypeptides. The major peroxisomal membrane proteins as well as most of the minor ones are absent from the endoplasmic reticulum (ER). Conversely, most ER proteins are absent from peroxisomes. By electron microscopy, purified peroxisomal membranes are ~6.8 nm thick and have a typical trilaminar appearance. The phospholipid/protein ratio of peroxisomal membranes is ~200 nmol/mg; the principal phospholipids are phosphatidyl choline and phosphatidyl ethanolamine, as in ER and mitochondrial membranes. In contrast to the mitochondria, peroxisomal membranes contain no cardiolipin. All the membranes investigated contain a polypeptide band with a molecular mass of ~15,000 daltons. Whether this represents an exceptional common membrane protein or a coincidence is unknown. The implications of these results for the biogenesis of peroxisomes are discussed.
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U2 - 10.1083/jcb.93.1.103
DO - 10.1083/jcb.93.1.103
M3 - Article
C2 - 7068748
AN - SCOPUS:0020039867
SN - 0021-9525
VL - 93
SP - 103
EP - 110
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 1
ER -