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K E Bloch

Publications and source records attributed to K E Bloch.

5 recordsLinked to original sources

Noninvasive measurement of central venous pressure by neck inductive plethysmography.

Bedside estimation of the height at which the internal jugular veins collapse, referenced to a standard hemodynamic location, theoretically reflects central venous pressure. This method has never been demonstrated as accurate when compared to invasive CVP measurements because of the great clinical skills and time required to visually identify the internal jugular venous waveform. Since the principles of the bedside method are sound, we utilized them in conjunction with the neck inductive plethysmograph, a device which has the capability of recording internal jugular venous and carotid arterial waveforms. The respiratory distortion of these vascular waveforms was eliminated by employing a digital bandpass filter, making it easy to identify the venous and arterial waveforms on the videoscreen of a personal computer. The upper torso was positioned while observing the videoscreen until the vascular waveform was seen as a mixed arteriovenous waveform, signifying intermittent internal jugular venous collapse. The height of the internal jugular vein above the phlebostatic axis was obtained by external measurement and recorded as CVPni in cm H2O. In 43 patients, 86 percent of CVPni (NIP) values fell within 20 percent CVPi (invasive catheter measurements) over a range of CVP from 0 to 19 cm H2O. In an additional seven patients, CVPi was greater than the height that the upper torso could be elevated and an arterial waveform could not be obtained. Here, CVPni was recorded as the value at least exceeding the value measured. In two other patients, obstruction of an internal jugular vein gave spuriously low values of CVPni. Our study indicates that this new neck inductive plethysmographic method is accurate compared to invasive catheter measurements of CVP and should serve as a safe, noninvasive alternative in situations where such measurements are required.

Adult

Speculations on the evolution of sterol structure and function.

The essential oxygen requirement for sterol biosynthesis dates this molecule as a relative latecomer in cellular evolution. Structural details of the cholesterol molecule and related sterols can be rationalized in terms of optimal hydrophobic interactions between the planar sterol ring system and phospholipid acyl chains in the membrane bilayer. The prediction that the cholesterol precursor lanosterol (4,4',14 trimethyl cholastadienol) is incompetent for membrane function is verified by in vivo experiments with eucaryotic sterol auxotrophs and microviscosity measurements of sterol-containing artificial membranes. For procaryotic cells the sterol specificity is very much broader. Methylococcus capsulatus produces 4,4-dimethyl- and 4-monomethyl sterols, but not sterols of the cholesterol type. Similarly lanosterol and its partially demethylated derivatives satisfy the sterol requirement of Mycoplasma capricolum. A more primitive but unspecified role of cyclized squalene derivatives is therefore postulated for procaryotic membranes. The finding that cholesterylmethyl ether satisfies the sterol requirement of certain microbial systems is at variance with current views on the role played by the sterol hydroxyl group in membrane organization and function.

Biological Evolution

Effect of a supernatant protein on microsomal squalene epoxidase and 2,3-oxidosqualene-lanosterol cyclase.

Squalene epoxidation catalyzed by rat liver microsomes requires oxygen NADPH, and the 105,000 x g supernatant (S105). The supernatant can be replaced by a partially purified S105 protein (SPF) and phospholipids (Tai, H., and Bloch, K. (1972) J. Biol. Chem. 247, 3767). When washed microsomes are preincubated anaerobically with [14C]squalene and S105 without NADPH, followed by centrifugation and washing to remove the unbound squalene and S105, epoxidation in the presence of O2 and NADPH occurs subsequently at the same rate as in direct assays containing all required components from the start. Partially purified SPF (65-fold) shows the same effect. Washed microsomes preincubated anaerobically with squalene alone, or with bovine serum albumin instead of S105, also take up large amounts of squalene, but the squalene so incorporated is only poorly converted to epoxide. The epoxidation of endogenous squalene formed in liver homogenates from [14C]mevalonate is also stimulated by S105. The incorporation of squalene into microsomes is temperature dependent. 2,3-Oxidosqualene-lanosterol cyclase (cyclase) also requires S105 for optimal activity. It is suggested that the S105 protein acts internally within the microsomal membrane system facilitating the access of substrate to specific enzyme sites.

Animals

COENZYME A.

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Acetylene