Amino Acid Composition and Terminal Sequences of Golfingia gouldii Hemerythrin^*

Abstract

The amino acid composition of the hemerythrin from the sipunculid worm Golfingia gouldii is, in residues per molecule of protein subunit of 13,500 molecular weight: Lysu.o,

Molecular variants of Golfingia gouldii hemerythrin. Primary structure of the variants arising from five amino acid interchanges

“…The carboxyl-terminal sequences of peptides were determined by carboxypeptidase A digestion and amino terminal residues were determined by digestion with leucine aminopeptidase or by the dansyl chloride reaction. Carboxypeptidase A digestion was performed as described by Groskopf et al (1966a). Amino acids liberated at various times from 2 to 22 hr were detected by automatic amino acid analysis.…”

The aminoterminal sequence of Dendrostomum pyroides hemerythrin

“…The sequence determined for the aminoterminal region ofD. pyroides hemerythrin is given in table 1 together with the sequence determined by Klotz and coworkers [1][2][3][4] for this portion of the pigment from Golfingia gouldii. These sequences are identical except for residues 9, 10 and 11.…”

“…G. gouldii were from the Marine Biological Laboratory, Woods Hole, Massachusetts. Hemerythrin was prepared as described previously [5] and converted to the apoprotein by the method of Groskopf et al [1 ]. Samples of the apohemerythrin (225 nmoles) were sequenced by Edman degradation using a Beckman-Spinco Protein/ Peptide Sequencer Model 890.…”

“…The pigment has a molecular weight of 107,000 and is composed of 8 subunits. The only sequence information available is for the subunit of the hemerythrin from the sipunculid worm Golfingia gouMii [1][2][3][4]. We have described earlier the properties of the hemerythrin from the sipunculid Dendrostomum pyroides [5 ] and now report the sequence of the first 35 aminoterminal residues of this protein.…”

Studies on Reduced Wool VIII. N-Acetyl Peptides Isolated From A Major Component

“…(e) Behaviour of Both peptides gave two incompletely separated peaks on Sephadex G-25 which had identical amino acid analyses and the most probable explanation is that one has the O-terminal Phe on the a-aspartyl carboxyl group and one has the O-terminal Phe on the ,B-aspartyl carboxyl group (cf. Groskopf et al 1966).…”