Pachystegia rufa and allied rock daisies : rarity and threats
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Threatened and uncommon plants of New Zealand
Abstract A reappraisal of the conservation status of the indigenous New Zealand vascular plant flora is presented. The list comprises 792 taxa (34% of New Zealand's total indigenous vascular flora) in the following categories: Extinct 4 taxa, Acutely Threatened 122 taxa (comprising 47 taxa Nationally Critical, 54 Nationally Endangered, 21 Nationally Vulnerable), Chronically Threatened 96 taxa (comprising Serious Decline 26 taxa, Gradual Decline 70 taxa), At Risk 499 taxa (comprising Sparse 126 taxa, Range Restricted 373 taxa), Non‐resident Native 26 taxa (comprising Vagrant 16 taxa, Colonist 10 taxa), and Data Deficient 45 taxa. A further 208 plants are listed as Taxonomically Indeterminate, being those which might warrant further conservation attention once their taxonomic status is clarified. A further 31 named taxa and 18 rated as Taxonomically Indeterminate, and previously considered to be threatened and/or uncommon, are removed from this updated listing. A concordance of plant names is provided. The lists presented use a new threat classification system developed by the New Zealand Department of Conservation for sole use within this country. This paper represents the first time the entire known indigenous vascular flora has been assessed from a conservation perspective since the mid 1970s. A brief analysis of the patterns of rarity exhibited by the taxa listed is presented.
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.