We tested the hypothesis that the dietary energy-dependent alterations of the rumen papillae size are accompanied by corresponding changes in systemic insulin-like growth factor (IGF)-1 concentration and in rumen papillary IGF type 1 receptors (IGF-1R). Young male goats (n=24) were randomly allocated to two groups (n=12) and fed a high level (HL) metabolizable energy [1200 kJ/(kg(0.75).d)] or a low level (LL) [500 kJ/(kg(0.75).d)] diet for 42 d. The concentration of ruminal total SCFA did not differ between the groups, but the molar proportion of butyric acid was enhanced by 70% in the HL group (P<0.05). Both the length and width of the papillae were greater (P<0.05) in the HL group, and the surface was 50-100% larger (P<0.05) in the tissue sampled from the artrium ruminis, the ventral ruminal sac and the ventral blind sac. Transport of Na+ across the rumen epithelium, which is amiloride sensitive, was higher (P<0.05) in the HL than in the LL group. Furthermore, the plasma IGF-1 concentration was about twofold higher in the HL group (P<0.05), and the maximal rumen epithelial IGF-1R binding was also higher in the HL (P<0.05) than in the LL group. IGF-1R mRNA and IGF-1 mRNA were detected in rumen papillae; however, they were unaffected by dietary treatments. DNA synthesis and cell proliferation of cultured rumen epithelial cells were higher (P<0.05) after IGF-1 treatment (25 or 50 microg/L) compared with those in the medium without IGF-1. Thus dietary energy-dependent alterations of rumen morphology and function are accompanied by corresponding changes in systemic IGF-1 and ruminal IGF-1R.

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A series of ribosomal subparticles derived from the 50S subunit has been studied and compared in EF-T- and EF-G-dependent reactions. Three different 50S cores were prepared by CsC1 isophycnic centrifugation and one by NH(4)Cl-ethanol extractionm the 50S CsCl core a had lost proteins L1, L7, L8, L10, L12, L16, L25, L33, and some L6 and L11. The 50S CsCl core b additionally lacked protein L6, and 50S CsCl core c also lacked protein L5, L15, L18, L27, L28, L30, and most of L9, L14, L19, and L21. The 50S NH(4)Cl-ethanol core had lost up to 90 percent of proteins L7, L12 and 30-60 percent of proteins L8, L10, and L29. The 50S CsCl core a had much reduced activity in EF-G and none in EF-T GTPase reactions while 50S CsCl cores b and c were inactive. Addition of proteins L7, L12 restored the activity for both the EF-T- and EF-G-dependent GTPase with all of the three 50S CsCl cores, increasing stepwise from core c to core a; The 50S NH(4)Cl-ethanol core was partially active in the EF-G GTPase over the 2-30 mM MG-2+ range tested, while EF-T only showed some activity inthe upper portion of this range...

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The main purpose of this note is to prove Miyadera's theorem on perturbations of semigroup generators (Miyadera [4]; see Remark 2, c) below) under reduced assumptions. In our proof we obtain the perturbed semigroup by an iteration similar to the iteration used in the proof for bounded perturbations. By an example we show that the theorem is optimal with respect to a constant occurring in the theorem.In the followingX will be a Banach space. (t)H < Le ~ (t ~ 0). The linear operator T defined by D(T)" = { x e X ; T x : = lim t -' ( W ( t ) -I ) x

The cell wall of the unicellular green alga Chlamydomonas reinhardtii consists predominantly of Hyp-rich glycoproteins, which also occur in the extracellular matrix of multicellular green algae and higher plants. In addition to the Hyp-rich polypeptides, the insoluble glycoprotein framework of the Chlamydomonas cell wall contains minor amounts of 14-3-3 proteins, as revealed by immunochemical studies and mass spectroscopic analysis of tryptic peptides. Polypeptides immunologically related to the 14-3-3 proteins also were found in the culture medium of Chlamydomonas. The levels of two of these 14-3-3-related polypeptides were decreased in the culture medium of the wall-deficient mutant cw-15 . These findings indicate that 14-3-3 proteins are involved in the cross-linking of Hyp-rich glycoproteins in the Chlamydomonas cell wall.

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