Versuche zur somatischen Beeinflussung der Organbildung pflanzlicher Embryonen
Experiments on influencing cotyledon formation in embryos ofEranthis hiemalis are reported. By treating the seeds with 100–2000 ppm solutions of 2,4-dichlorophenoxyacetic acid, 2,4,5-trichlorophenoxyacetic acid, 2-methyl-4-chlorophenoxyacetic acid, α-naphthylacetic acid and even isopropyl N-phenyl carbamate one can obtain significant increases in twinning and in cotyledon anomalies (syncotyly and pleiocotyly of all degrees). Embryos can be successfully treated until approximately 2 weeks after initial opening of the follicles. X-radiations achieve the same effect, with doses of 2000–4000r corresponding to the treatments with 1000–2000 ppm 2,4-D-solutions. By using weaker concentrations and with sudden temperature changes one can likewise raise the percentage of syn-, tri- and tetracotyls, but pleiocotyls of the higher degrees (5 and more cotyledons) appear only when more intensive methods of treatment are employed. These forms which exceed the normal range of variability arise as bud-like embryo regenerates on the as yet undifferentiated original embryo.
Influence of Position of Truss on Pleiocotyly in Tomato
LEWIS1 has shown that position of truss affects the manifestation of rogues in tomato. Darlington and Mather2 believe this character is plasmagenically inherited, like other forms of rogues in inbreeding species. An investigation was therefore made to determine whether truss position and plasmagenes also influence pleiocotyly, that is, the variation in cotyledon number, in tomato (Lycopersicon esculentum).
On the fractionation of β-lactoglobulin and α-lactalbumin
Abstract Existing methods for the preparation of α-lactalbumin and β-lactoglobulin are examined critically. It is proposed that the most satisfactory method for the preparation of the whey protein fraction from bovine milk is (NH 4 ) 2 SO 4 fractionation. A number of new gentle procedures for the fractionation of the whey proteins are compared with some existing methods. The distribution of total protein at various stages is determined by total Kjeldahl nitrogen and the kind of protein by starch-gel electrophoresis. The effect of variables, such as pH, salt concentration and temperature on the separation of α-lactalbumin and serum albumin from β-lactoglobulin is studied. Differences in the behavior ( e.g. solubility) of genetic variants of β-lactoglobulin are noted. The solubility of each of the major whey proteins, under similar conditions to those used in the fractionation, is compared with its solubility in the whey protein mixture. The understanding gained of factors important in the fractionation is used in recommending new procedures for α-lactalbumin and β-lactoglobulin isolation.