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F Northrop

Publications and source records attributed to F Northrop.

5 recordsLinked to original sources

A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme.

The aim of this work was to identify enzymes that participate in the degradation of transitory starch in Arabidopsis. A mutant line was isolated by screening leaves at the end of the night for the presence of starch. The mutant had a higher starch content than the wild-type throughout the diurnal cycle. This accumulation was due to a reduction in starch breakdown, leading to an imbalance between the rates of synthesis and degradation. No reduction in the activity of endo-amylase (alpha-amylase), beta-amylase, starch phosphorylase, maltase, pullulanase or D-enzyme could be detected in crude extracts of leaves of the mutant. However, native PAGE in gels containing amylopectin revealed that a starch-hydrolysing activity, putatively identified as an endo-amylase and present in wild-type chloroplasts, was absent or appreciably reduced in the mutant. This is the first time that a specific enzyme required for starch degradation has been identified in leaves.

Amylases↗

Characterization and properties of a modified human interferon-alpha containing an additional 18 amino acids at the N-terminus.

A modified human interferon-alpha 2 was produced in Escherichia coli cells infected with phage M13 mp7 containing an interferon-alpha gene. After purification by immunochromatography with the monoclonal antibody NK2, the N-terminal amino acid sequence was determined. The N-terminal methionine was absent but an additional sequence of 18 amino acids at the N-terminus was retained. The modified interferon-alpha 2 was indistinguishable from authentic interferon-alpha 2 in its ability to activate natural killer cells, to slow the growth of Daudi cells, and to confer virus resistance on heterologous cells.

Amino Acid Sequence↗

N-terminal amino acid sequence of a human delta-chain myeloma protein.

The N-terminal amino acid sequence (26 residues) of a delta-chain of a human myeloma (Er I) is homologous with the prototype sequence of the human VHIII subgroup. This indicates that the delta-chain is using for its V region the same pool of V genes as the rest of the immunoglobulin classes. Implications of this finding are discussed.

Amino Acid Sequence↗