Chow YW, Pietranico R, Mukerji A. Studies of oxygen binding energy to hemoglobin molecule. Biochem Biophys Res Commun 1975;66(4):1424-31.
Takagi Y, Shikita M. The active form of cytochrome P-450 from bovine adrenocortical mitochondria. J Biol Chem 1975;250(21):8445-8.Abstract
Cytochrome P-450 from bovine adrenocortical mitochondria exists in three forms of molecular weight: 850,000 (protein 16), of one-half (protein 8), and of one-quarter of this value (protein 4). The forms of the enzyme are named according to the number of subunits and all appear to be active in converting cholesterol to 3beta-hydroxy-5-pregnen-20-one (side chain cleavage) (Shikita, M., and Hall, P.F. (1973) J. Biol. Chem. 248, 5606). To determine whether all three forms are active at their characteristic molecular weights, the three cytochromes were each layered onto separate sucrose density gradients and centrifuged at 49,000 rpm for 60 min; the gradients contained all the factors necessary for side chain cleavage including one of the following substrates: cholesterol, 20S-hydroxycholesterol, and 20S,22R-dihydroxycholesterol. Regardless of the form of P-450 layered onto the gradient and regardless of the substrate, enzyme activity (side chain cleavage) was observed only in fractions corresponding to a sedimentation coefficient of 20 to 22 S which is that for protein 16. No activity was observed at S values corresponding to either protein 8 or protein 4. These findings indicate that the active form of cytochrome P-450 from adrenocortical mitochondria is that containing 16 subunits, i.e. the form in which the cytochrome is normally isolated from adrenal mitochondria. Forms consisting of eight and four subunits which can be prepared from protein 16 become active only by forming protein 16, at least in an aqueous medium in vitro.
Bose KS, Sarma RH. Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution. Biochem Biophys Res Commun 1975;66(4):1173-9.
Schmoldt A, Benthe HF, Haberland G. Digitoxin metabolism by rat liver microsomes. Biochem Pharmacol 1975;24(17):1639-41.
Makar AB, McMartin KE, Palese M, Tephly TR. Formate assay in body fluids: application in methanol poisoning. Biochem Med 1975;13(2):117-26.
Lefkowitz RJ. Identification of adenylate cyclase-coupled beta-adrenergic receptors with radiolabeled beta-adrenergic antagonists. Biochem Pharmacol 1975;24(18):1651-8.
Akamatsu N, Nakajima H, Ono M, Miura Y. Increase in acetyl CoA synthetase activity after phenobarbital treatment. Biochem Pharmacol 1975;24(18):1725-7.
Turner AJ, Hick PE. Inhibition of aldehyde reductase by acidic metabolites of the biogenic amines. Biochem Pharmacol 1975;24(18):1731-3.
Eickenroht EY, Gause EM, Rowlands JR. The interaction of SO2 with proteins. Environ Lett 1975;9(3):265-77.
Durbin RP. Letter: Acid secretion by gastric mucous membrane. Am J Physiol 1975;229(6):1726.
Thornton JA, Harrison MJ. Letter: Duration of action of AH8165. Br J Anaesth 1975;47(9):1033.
Randerson, James T, Slotkin TA. Maturation of the adrenal medulla--IV. Effects of morphine. Biochem Pharmacol 1975;24(16):1469-74.
Smith RJ, Bryant RG. Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem Biophys Res Commun 1975;66(4):1281-6.
Kawai T, Yamada Y, Tsuneda J, Aoyagi T, Mikata A. Pleural effusion associated with aortitis syndrome. Chest 1975;68(6):826-8.Abstract
A patient with aortitis syndrome had a pleural effusion which subsided but reappeared with an exacerbation of aortitis symptoms while under antituberculosis treatment. The character of the fluid was that of an exudate, and the glucose concentration was normal. Clinical and laboratory features of the case suggest that the effusion was part of the aortitis syndrome per se.
Chow YW, Pietranico R, Mukerji A. Studies of oxygen binding energy to hemoglobin molecule. Biochem Biophys Res Commun 1975;66(4):1424-31.