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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Bibliographic Details
Published inComparative biochemistry and physiology Vol. 31; no. 1; pp. 55 - 64
Main Authors Terwilliger, Robert C., Read, Kenneth R.H.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 01.10.1969
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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.
ISSN:0010-406X
DOI:10.1016/0010-406X(69)92168-9