Abstract
1. 1. Amino acid sequences of the soluble tryptic peptides of yellowfin tuna myoglobin, comprising 60% of the total residues, are presented. 2. 2. The amino terminus is acetylated as shown by Fourier transform nuclear magnetic resonance spectroscopy of an N-terminal dipeptide. 3. 3. Comparison of peptide sequences from yellowfin tuna myoglobin with corresponding regions of mammalian myoglobins shows obvious homology around the heme-attachment site and the carboxyl terminus, but marked dissimilarity is evident at other locations, such as the amino terminal region.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 481-487 |
| Number of pages | 7 |
| Journal | Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
| Volume | 62 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1979 |
Fingerprint
ASJC Scopus subject areas
- Medicine(all)
Cite this
Sequences of the soluble tryptic peptides from myoglobin of yellowfin tuna (Thunnus albacares). / Rice, Robert H.; Watts, Daniel A.; Duane Brown, W.
In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 62, No. 4, 1979, p. 481-487.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sequences of the soluble tryptic peptides from myoglobin of yellowfin tuna (Thunnus albacares)
AU - Rice, Robert H.
AU - Watts, Daniel A.
AU - Duane Brown, W.
PY - 1979
Y1 - 1979
N2 - 1. 1. Amino acid sequences of the soluble tryptic peptides of yellowfin tuna myoglobin, comprising 60% of the total residues, are presented. 2. 2. The amino terminus is acetylated as shown by Fourier transform nuclear magnetic resonance spectroscopy of an N-terminal dipeptide. 3. 3. Comparison of peptide sequences from yellowfin tuna myoglobin with corresponding regions of mammalian myoglobins shows obvious homology around the heme-attachment site and the carboxyl terminus, but marked dissimilarity is evident at other locations, such as the amino terminal region.
AB - 1. 1. Amino acid sequences of the soluble tryptic peptides of yellowfin tuna myoglobin, comprising 60% of the total residues, are presented. 2. 2. The amino terminus is acetylated as shown by Fourier transform nuclear magnetic resonance spectroscopy of an N-terminal dipeptide. 3. 3. Comparison of peptide sequences from yellowfin tuna myoglobin with corresponding regions of mammalian myoglobins shows obvious homology around the heme-attachment site and the carboxyl terminus, but marked dissimilarity is evident at other locations, such as the amino terminal region.
UR - http://www.scopus.com/inward/record.url?scp=0018404424&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018404424&partnerID=8YFLogxK
U2 - 10.1016/0305-0491(79)90121-4
DO - 10.1016/0305-0491(79)90121-4
M3 - Article
C2 - 318454
AN - SCOPUS:0018404424
VL - 62
SP - 481
EP - 487
JO - Comparative biochemistry and physiology. B, Comparative biochemistry
JF - Comparative biochemistry and physiology. B, Comparative biochemistry
SN - 1096-4959
IS - 4
ER -