Quaternary structure of the radular muscle myglobin of the gastropod mollusc buccinum undatum L
1. 1. The radular muscle myoglobin of the gastropod mollusc Buccinum undatum has been purified. 2. 2. The myoglobin has a molecular weight of 33,800 and possesses two heme groups per molecule. 3. 3. When the myoglobin is reacted with excess p-hydroxymercuribenzoate (PMB), a single derivative of mole...
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Published in | Comparative biochemistry and physiology Vol. 31; no. 1; pp. 55 - 64 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
01.10.1969
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Subjects | |
Online Access | Get full text |
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Summary: | 1.
1. The radular muscle myoglobin of the gastropod mollusc
Buccinum undatum has been purified.
2.
2. The myoglobin has a molecular weight of 33,800 and possesses two heme groups per molecule.
3.
3. When the myoglobin is reacted with excess
p-hydroxymercuribenzoate (PMB), a single derivative of molecular weight 16,900 is formed.
4.
4. The amino acid composition of the purified PMB derivative is: Lys
18His
7 Arg
2 Asp
16 Thr
14 Ser
8 Glu
5 Pro
2 Gly
13 Ala
19
1
2
Cys
2
Val
5 Met
5 Ileu
3 Leu
17 Tyr
1 Phy
10 Trp
3
.
5.
5. The native myoglobin is probably composed of two identical subunits.
6.
6. When the PMB-derivative is reacted successively with 2-mercaptoethanol and aminoiminoemethanesulfinic acid, a dimeric myoglobin is regenerated.
7.
7. The evolutionary relationship of
Buccinum myoglobin to other gastropod myoglobins is discussed. |
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ISSN: | 0010-406X |
DOI: | 10.1016/0010-406X(69)92168-9 |