Biomedical subjects

Maggie Smallwood

Publications and source records attributed to Maggie Smallwood.

3 recordsLinked to original sources

PubMed2005

Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.).

Recrystallisation inhibition (RI) activity has been isolated from cold-acclimated Forsythia suspensa bark and leaves, which is stable when boiled, and not sensitive to reducing agents. The antifreeze activity has been purified to a single 20 kDa protein, using anion exchange, hydroxyapatite chromatography, and gel filtration. The protein is abundant in forsythia bark with 0.5microg pure protein obtained from 35 g bark. RI activity is seen with as little as 6 microg ml(-1) protein. Sequence homology was seen with dehydrins, and forsythia AFP contains the Y-segment, a conserved region found in many dehydrins.

Amino Acid Sequence↗

PubMed2002

Plants in a cold climate.

Plants are able to survive prolonged exposure to sub-zero temperatures; this ability is enhanced by pre-exposure to low, but above-zero temperatures. This process, known as cold acclimation, is briefly reviewed from the perception of cold, through transduction of the low-temperature signal to functional analysis of cold-induced gene products. The stresses that freezing of apoplastic water imposes on plant cells is considered and what is understood about the mechanisms that plants use to combat those stresses discussed, with particular emphasis on the role of the extracellular matrix.

Acclimatization↗

PubMed2002

The stability during low-temperature storage of an antifreeze protein isolated from the roots of cold-acclimated carrots.

Natural antifreeze proteins (AFPs) not only inhibit freezing at high subzero temperatures; they have the additional properties of inhibiting the recrystallization of ice during warming and of preventing devitrification. The natural AFP that occurs in the roots of cold-acclimated carrots can be extracted reasonably simply and is non-toxic: it was selected for study as a possible ingredient of the vitrification mixtures that are being developed for use in tissue cryopreservation. For this application, it would be essential for the AFP to remain active during prolonged storage at very low temperatures. For logistic reasons, it would also be essential to have an effective method of storage of the purified AFP itself. In this study, carrot AFP was isolated and purified, and its ability to inhibit recrystallization was monitored over 40 weeks of storage at -80 or -196 degrees C. The data revealed a progressive decrease in activity during storage, reaching half the original activity in 10-20 weeks and only 2-3% of the original activity at 40 week. These data suggest that carrot AFP will not be effective in tissue cryopreservation.

Antifreeze Proteins↗