The effect of bond structure on the Baker–Venkataraman transformation of acetylanisoyloxyindanes and benzoyloxytetrahydroacetonaphthones

O'Farrell, M. P.; Wheeler, Desmond M. S.; Wheeler, Margaret M.; Wheeler, T. S.

doi:10.1039/jr9550003986

Cited by 12 publications

(11 citation statements)

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“…The actins showed better than 90 % purity as judged by electrophoresis on polyacrylamide gels in the presence of dodecylsulphate [15]. The actins showed both the p and y species upon isoelectric focusing in the presence of 9 M urea and NP40 as described by O'Farrell [16]. (These analyses have been kindly performed by Dr K.…”

Section: Actins From Calf Thymus and Bovine Brainmentioning

confidence: 94%

Actin Amino-Acid Sequences. Comparison of Actins from Calf Thymus, Bovine Brain, and SV40-Transformed Mouse 3T3 Cells with Rabbit Skeletal Muscle Actin

1978

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Actin was purified from calf thymus, bovine brain and SV40-transformed mouse 3T3 cells grown in tissue culture. Isoelectric focusing analysis showed the presence of the two actin polypeptides p and y typical for non-muscle actins in all three actins. Tryptic and thermolytic peptides accounting for the complete amino-acid sequence of the cytoplasmic actins were separated and isolated by preparative fingerprint techniques. All peptides were characterized by amino-acid analysis and compared with the corresponding peptides from rabbit skeletal muscle actin. Peptides which differed in amino-acid composition from the corresponding skeletal muscle actin peptides were subjected to sequence analysis in order to localize the amino-acid replacement. The results obtained show that all three mammalian cytoplasmic actins studied contain the same amino-acid exchanges indicating that mammalian cytoplasmic actins are very similar if not identical in amino-acid sequence.The presence of two different isoelectric species p and 1' in cytoplasmic actins from higher vertebrates is accounted for by the isolation of two very similar but not identical amino-terminal peptides in all three actin preparations. The nature of the amino-acid replacements in these two peptides not only accounts for the different isoelectric forms but also shows that p and y cytoplasmic actins are the products of two different structural genes expressed in the same cell. The total number of aminoacid replacements so far detected in the comparison of these cytoplasmic actins and skeletal muscle actin is 25 for the p chain and 24 for the y chain. With the exception of the amino-terminal three or four residues, which are responsible for the isoelectric differences, the replacements do not involve charged amino acids. The exchanges are not randomly distributed. No replacements were detected in regions 18 -75 and 299 -356 while the regions between residues 2 -17 and 259 -298 show a high number of replacements.In addition documentation for a few minor revisions of the amino acid sequence of rabbit skeletal muscle actin is provided

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Section: Actins From Calf Thymus and Bovine Brainmentioning

confidence: 94%

Actin Amino-Acid Sequences. Comparison of Actins from Calf Thymus, Bovine Brain, and SV40-Transformed Mouse 3T3 Cells with Rabbit Skeletal Muscle Actin

1978

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“…Two-dimensional gels were run as described by O'Farrell (1975). Acrylamide gel mix for the first dimension contained urea (9.5 M), acrylamide 4% (w/v), NP40 (2% v/v), ampholines (Pharmacia, Milton Keynes, UK) pH 3.5-10 (3% v/v) and ampholines pH 5-7 (2% v/v): this was polymerized in 10.5-cm tubes.…”

Section: Sds -Page Gels and Western Blotsmentioning

confidence: 99%

Common components of the infection thread matrix and the intercellular space identified by immunocytochemical analysis of pea nodules and uninfected roots

et al. 1989

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Three rat hybridoma cell lines have been isolated which produce monoclonal antibodies identifying a noduleenhanced, soluble component of Pisum sativum root nodules. These antibodies each recognized a protease‐sensitive band (Mr 95K) on SDS‐polyacrylamide gels. The 95K antigen was resolved by isoelectric focusing into acidic and neutral components which were separately detected by AFRC MAC 236 and MAC 265 respectively. The third antibody (MAC 204) reacted with both acidic and neutral components through an epitope that was sensitive to periodate oxidation. These monoclonal antibodies were used for immunogold localizations at light and electron microscopic levels. In each case, the antigen was shown to be present in the matrix that surrounds the invading rhizobia in infection threads and infection droplets, as well as in the intercellular spaces between plant cell walls of nodules and also of uninfected roots. By contrast, a fourth monoclonal antibody, AFRC JIM 5, labelled a pectic component in the walls of infection threads, and JIM 5 was also found to label the middle lamella of plant cell walls, especially at three‐way junctions between cells. The composition and structure of the infection thread lumen is thus comparable to that of an intercellular space.

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“…SDS-PAGE was p~ribrmed as de~erib~ in [9]. 10/ag of protein were applied on a linear gradient g~l, 10-15% w/v with 4.5% w/v .~taeking gel, A 45 mA constant current was applied for 3 h. The pl (17-04714)1) and molecular weight markers (17-0446-01)were purcha.~ed from Pharmacia.LKB.…”

Section: Methodsmentioning

confidence: 99%

Generation of Gla‐domainless FVIIa by cathepsin G‐mediated cleavage

Nicolaisen¹,

Petersen²,

Thim³

et al. 1992

FEBS Letters

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Coagulation factor VII contains ten ~,.carbox),glutamic acid residues in the N-terminal region (Gla-domailO which are essential for the hemostatie function of FVII. The pre~ent study shows that granulocyte cathepsin G degrades the Gla-domain of FVlla in vitro. Characterization of the truncated FVIIa by SDS-PAGE and N-terminal amino acid sequence analysis revealed that cleavage had occurred between Tyr-44 and Ser-45 and that further cleavage was only obtained on e~tensive cathepsin G exposure. Cleavage of vitamin K-dependent coagulation factors by ¢athepsin G may play a role in vivo, and it offers a convenient way of obtaining proteitas deprived of their Gin-domain for functional and structural studies.

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The effect of bond structure on the Baker–Venkataraman transformation of acetylanisoyloxyindanes and benzoyloxytetrahydroacetonaphthones

Cited by 12 publications

References 0 publications

Actin Amino-Acid Sequences. Comparison of Actins from Calf Thymus, Bovine Brain, and SV40-Transformed Mouse 3T3 Cells with Rabbit Skeletal Muscle Actin

Actin Amino-Acid Sequences. Comparison of Actins from Calf Thymus, Bovine Brain, and SV40-Transformed Mouse 3T3 Cells with Rabbit Skeletal Muscle Actin

Common components of the infection thread matrix and the intercellular space identified by immunocytochemical analysis of pea nodules and uninfected roots

Generation of Gla‐domainless FVIIa by cathepsin G‐mediated cleavage

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