Key points are not available for this paper at this time.
A species of cytochrome b(5) with a monomer molecular weight of 16,700 has been isolated from rabbit-liver microsomes by a procedure that uses detergents and avoids the use of any proteolytic or lipolytic enzymes. This detergent-extracted cytochrome b(5) is larger than the trypsin- or lipase-extracted enzyme, and appears to contain an extremely hydrophobic appendage of 40 amino acids, probably at the N-terminus. The hydrophobic character of the extra amino acid sequence leads to aggregation in the absence of detergents, and may be of considerable importance in the binding of the enzyme to microsomes. It is suggested that the hydrophilic portion of the cytochrome molecule, which bears the heme and is enzymatically functional, is oriented toward the surface of the membrane where it readily reacts with nonmicrosomal proteins, while the hydrophobic "tail" anchors the heme protein tightly to the membrane.
Spatz et al. (Sat,) studied this question.