A B S T R A C T Normal human volunteers were intubated with either aspiration tubes or a biopsy capsule placed in the small intestine. The subjects were then fed a test meal containing 50 g of purified bovine serum albumin which served as the model dietary protein.Electrophoretic analysis of intestinal fluids showed that for at least 4 h the fed albumin was detectable in jejunal and ileal fluids. On separate occasions, subjects were fed the same meal without the protein. No protein was detected in intestinal fluids when the protein-free meal was fed. After the protein-rich meal, total concentrations of measured free and peptide amino acids rose from 3.21 to 29.29, and 15.94 to 117.97 ,umol/ml, respectively, (P values <0.02) in the jejunum. Similarly, total concentrations of measured free and peptide amino acids rose from 5.45 to 19.74, and 13.59 to 65.39, respectively, (P values < 0.05) in the ileum. In contrast, concentrations of free and peptide amino acids in intestinal fluids did not increase after the protein-free meal. While intracellular concentrations of amino acids in the jejunal mucosa did not show significant changes, plasma concentrations of each individual free amino acid were increased after the protein-rich meal and were either decreased or unaltered after the proteinfree meal. The amino acid composition of the fed protein was reflected in the increases in intraluminal and plasma concentrations of individual amino acids after the protein-rich meal. It is concluded that after the ingestion of a test meal containing a substantial amount of protein which is within the usual range of dietary

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Lactic dehydrogenase (LD) isoenzymes were determined by a rapid, simple technique and their utility in the diagnosis of acute myocardial infarction (AMI) was evaluated. LD isoenzymes were separated by ion-exchange column chromatography using DEAE-Sephadex. The cardiac fractions (LD-1 and LD-2) were measured separately on an Abbott ABA-100 analyzer and ratio of LD isoenzyme 1 to LD isoenzyme 2 (LD1:2) calculated. Daily serum samples were obtained from 100 patients selected only for a history of chest pain of abrupt onset. In 47 patients whose diagnosis was acute myocardial infarction (AMI), confirmed by typical clinical presentation and typical rise in cardiac-specific creatine kinase isoenzyme (MB(, peak LD1:2 ranged from 0.77 to 2.26. In 44 patients without AMI, peak LD1:2 ranged from 0.25 to 0.76. In two patients with electrocardiographic changes chest pain occurred two and five days previously; there was no rise in MB, but LD1:2 was elevated. Four patients with small AMI had no rise in LD1:2. Three more patients (one with active hemolysis) had false positive results. Thus, there was a sensitivity of 96% and a specificity of 97% when the cut-off point was LD1:2 = 0.76. LD1:2 is not quite as sensitive or specific as MD, but the ratio allows for the diagnosis of infarction in cases where MB has already returned to normal.

I describe a simple, rapid anion-exchange column chromatographic technique for separating the creatine kinase (CK) isoenzymes in human serum and tissue. Extracts of CK-rich tissues (skeletal muscle, cardiac muscle, and brain) were used to determine optimum conditions for separating CK isoenzymes MM, MB, and BB. Samples, layered on mini-columns (0.5 x 6.0 cm) of DEAE-Sephadex A-50, were eluted stepwise with Tris-buffered sodium chloride (100, 200, and 300 mmol/Iiter). Column effluents were assayed by the Rosalki CK method. Distribution of total activity among the eluted fractions was tissue-specific and reproducible. Evaluation of sera from 71 patients with myocardial infarction and other diseases associated with elevated CK activity revealed isoenzyme patterns that resembled those of either cardiac muscle or skeletal muscle. Cardiac pattern (presence of MB isoenzyme) and clinical documentation of myocardial infarction were 100% correlated in the 35 patients so studied.