Amino acid utilization and isotope discrimination of amino nitrogen in nitrogen metabolism of rat liver in vivo.

Urea and plasma protein differ in natural 15N abundance up to 10%. The origin of this difference is the branched nitrogen metabolism in the liver. One main branch is the protein synthesis pathway, the other the urea synthesis pathway. By this branching 15N of precursor amino acids is depleted in urea while it is enriched in protein. With the 15N abundance of precursor amino acids, which may be taken from jejunum tissue, utilization of amino acids in liver metabolism can be calculated from isotope discrimination in either pathway. This was investigated by feeding different proteins to rats. When feeding high quality protein (whey protein) utilization of amino acids in liver metabolism at requirement intake was better than at zero protein intake (> 85% vs. 70%). From this we conclude that the pattern of amino acids available from the metabolic pool at zero protein intake is characterized by an imbalance. This endogenous imbalance can be complemented by exogenous dietary amino acids so that nitrogen excretion may even be smaller than the so-called "obligatory" losses of intakes not exceeding requirement. Thus, the quality of dietary protein is reflected not only by N balance. It also may be quantified by analysis of isotope discrimination in nitrogen metabolism of the liver. In addition, the quality of amino acid pattern available from the metabolic pool is indicated by this method.

Variable temperature UHV dual-range cell for spectroscopic surface studies.

A stainless steel cell for transmission spectroscopy of surface compounds is described. This cell allows subsequent spectra recording of the sample in two spectral regions requiring different window materials. The sample temperature can be varied from 100 to 700 K, the pressure from 10(-6) to 10(5) Pa. The mean temperatue is measured inside the wafer with a thin platinum wire as a resistance thermometer.