Ее чуть побольше в сети будет :-)

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Note added at 54 mins (2005-04-30 15:26:11 GMT)
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Источника, который однозначно сказал бы, что hydrophobic chromatography и hydrophobic interaction chromatography - синонимы, мне найти не удалось, но есть косвенные доказательства:

1) Исторический очерк в руководстве \"hydrophobic interaction chromatography\" с параграфом:

Hofstee and later Shaltiel proposed ‘‘hydrophobic chromatography’’ with the implicit assumption that the mode of interaction between proteins and the immobilized hydrophobic ligands is similar to the self association of small aliphatic organic molecules in water.

Далее рассуждения о развитии метода продолжаются, но нигде не указано, что hydrophobic interaction chromatography - принципиально иной метод

2) Статья, где оба термина используют взаимозаменяемо. Так, в одном параграфе, описывая исследование, говорят:

Cation-exchange chromatography on CM-Sephadexwas usedas a pre-fractionation step for the hydrolysate. VV-haemorphin-7 and VVhaemorphin-4 were eluted in two different fractions. The second and final purification step was hydrophobicinteraction chromatography on phenyl-Sepharose...

а потом, несколькими страницами ниже, детальнее расшифровывают:

We managed to fractionate the two haemorphins VVh4 and VVh7 in two different fractions, CM-2 and CM-3 respectively. Obviously, these fractions were not pure and hydrophobic chromatography was subsequently carried out on each fraction.

Вот.

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Note added at 1 hr 11 mins (2005-04-30 15:43:19 GMT)
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О хроматографиях гидрофобной и обращенно-фазной

HIC vs RPC

In theory, HIC and reverse-phase chromatography (RPC) are closely related LC techniques. Both are based upon interactions between solvent-accessible non-polar groups (hydrophobic patches) on the surface of biomolecules and the hydrophobic ligands (alkyl or aryl groups) covalently attached to the gel matrix. In practice, however, they are different. Adsorbents for RPC are more highly substituted with hydrophobic ligands than HIC adsorbents. The degree of substitution of HIC adsorbents is usually in the range of 10–50 mmoles/ ml gel of C2–C8 alkyl or simple aryl ligands, compared with several hundred mmoles/ml gel of C4–C18 alkyl ligands usually used for RPC adsorbents. Consequently, protein binding to RPC adsorbents is usually very strong, which requires the use of non-polar solvents for their elution. RPC has found extensive applications in analytical and preparative separations of mainly peptides and low molecular weight proteins that are stable in aqueous-organic solvents.

In summary, HIC is an alternative way of exploiting the hydrophobic properties of proteins, working in a more polar and less denaturing environment. Compared with RPC, the polarity of the complete system of HIC is increased by decreased ligand density on the stationary phase and by adding salt to the mobile phase.

Но, конечно, у нас могла закрепиться только обращенно-фазная...

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Note added at 2 hrs 43 mins (2005-04-30 17:15:50 GMT)
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Если у вас под рукой трехтомник \"Молекулярной биологии клетки\", то можете проверить, как мирцы перевели вот этот раздел в главе о методах


Название раздела:

Proteins Can Be Separated by Chromatography

Proteins are most often fractionated by column chromatography, in which a mixture of proteins in solution is passed through a column containing a porous solid matrix. The different proteins are retarded to different extents by their interaction with the matrix, and they can be collected separately as they flow out of the bottom of the column (Figure 8-10). Depending on the choice of matrix, proteins can be separated according to their charge (ion-exchange chromatography), ***their hydrophobicity (hydrophobic chromatography),*** their size (gel-filtration chromatography), or their ability to bind to particular small molecules or to other macromolecules (affinity chromatography).