No abstract

A comparison was made of the distribution of amino terminal end groups in the cellular proteins of a number of microbes. Among the procaryotes, methionine is a highly variable but virtually ubiquitous major protein end group. This is consistent with its possible role as a general amino acid initiator of protein biosynthesis in the procaryotes. Generally, however, alanine is the most abundant of the major end groups, followed in decreasing order by serine, threonine, the acidic amino acids, and occasionally lysine. No other new major end-groups were found. Among 15 representatives of the Enterobacteriaceae, retention of the initiating methionine terminus of the cellular protein varies considerably at a tribal level and is randomized at a familial level. The profiles of the five remaining end groups, however, are strikingly uniform, and are, for example, close to but significantly different from those of the Erwineae. Among the taxonomically more heterogeneous Bacillaceae, end-group profiles vary more and are sometimes unrelated. End-group analysis is thus particularly useful as a molecular criterion of taxonomy in assessing familial homogeneity. Free NH2 termini in eucaryote cell proteins are fewer, and they have increased acidic amino acid components and no methionine; they are otherwise similar to those of the procaryotes.

The morphology, host range, structural proteins and serological properties of Streptococcus thermophilus phages isolated from Finnish cheese plants were investigated. The results show that all the nine phages belong morphologically to Ackermann's group B1. The host-phage reactions and plating efficiency justify the division of these phages into four specificity groups. Most of the phages showed an absolute host specificity as to their plating efficiency but were not strictly specific in the adsorption to different hosts. The electrophoretic profiles of the structural proteins appeared nearly identical. Ten to eleven well separated proteins could be detected. The antiserum raised against one of the phages contained antibodies with different neutralization capacity depending on the phage. Using an immunoblotting technique, four structural proteins were detected that could bind phage antibodies.

High-titer lysates of a bacteriophage active against Lactobacillus lactis were prepared from liquid cultures as well as from areas of confluent lysis in soft-agar overlayers. Phage concentration and purification were accomplished by means of polyethylene glycol precipitation, differential centrifugation. The buoyant density of this phage in cesium chloride was 1.4795 g/ml. Characterization of phage growth cycle by one-step growth experiments under optimal conditions showed that the latent period was about 120 min, that the rise period lasted approx. 130 min, and that the average burst-size was about 80.

– Purified milk lactoperoxidase and endogenous human salivary peroxidase were used to label the proteins of whole mouth saliva with [125I]iodide. The proteins were then analyzed by isoelectric focusing or they were subjected so one‐dimensional polyacrylamide gel electrophoresis at pH 8.4. The radioactivity of the resolved protein fractions was determined. There were three to four major and four to five minor areas of radioactivity which were carried together with more or less distinctive protein fractions. Amylase and albumin were shown to be the most effective in binding [125I]iodide. No significant differences were observed in the iodination patterns of salivary proteins iodinated in the presence of endogenous saliva peroxidase and those iodinated in the presence of added milk lactoperoxidase. Hydrogen peroxide was necessary for iodination to take place. The significance of iodoproteins and the role of salivary peroxidases in the nonthyroidal metabolism of iodine are discussed.