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This article is a critique of the meaning and importance of some of the recently published work in the field whose development as a special area began with papers by Zuckerkandl & Pauling and Pauling & Zuckerkandl entitled Chemical Paleogenetics, Molecular Restoration Studies of Extinct Forms of Life and the paper by Margoliash on the evolution of cytochrome c. The primary emphasis is on conclusions and inferences derivable from amino acid sequences, followed bya section on nucleotide sequences. These are preceded by a brief indication of some of the literature that antedates the origin of the genetic code as it now stands. This will not treat immunoglobulin evolution, reviewed by Gally & Edelma and Smith, Hood & Fitch or related material on the evolution of enzymes and proteins reviewed by Smith and Arnheim. The functional interpretation of these changes has made significant progress [Dickerson and Takano et al]. For the evolution of metabolic pathways, see brew, Vogel, and Lejohn. [ABSTRACT FROM AUTHOR]

Amino acid analyses of L-lactate dehydrogenase from baker's show that the minimum molecular weight (53 000 daltons) of the protein is much lower than found in the literature (80 000). This result, combined with those reported in the following papers, leads to a revision of the dimeric model generally accepted for cytochrome b2 [ABSTRACT FROM AUTHOR]

Amino acid analyses of L-lactate dehydrogenase from baker's show that the minimum molecular weight (53 000 daltons) of the protein is much lower than found in the literature (80 000). This result, combined with those reported in the following papers, leads to a revision of the dimeric model generally accepted for cytochrome b2 [ABSTRACT FROM AUTHOR]

Ion-exchange chromatography of the total cytochrome c extracted from a wild-type laboratory strain of Saccharomyces cerevisiae shows the presence of two minor cytochrome c peaks, besides the already known iso-1 and iso-2 cytochromes c. Their amino acid composition is very similar to that of iso-1, but one of them lacks the ε-N-trimethylated lysine residue characteristic of yeast cytochromes c, thus excluding, at least for this peak, an artifactual origin. [ABSTRACT FROM AUTHOR]